31 results on '"Katherine E. Sloan"'
Search Results
2. The 5S RNP Couples p53 Homeostasis to Ribosome Biogenesis and Nucleolar Stress
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Katherine E. Sloan, Markus T. Bohnsack, and Nicholas J. Watkins
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Biology (General) ,QH301-705.5 - Abstract
Several proto-oncogenes and tumor suppressors regulate the production of ribosomes. Ribosome biogenesis is a major consumer of cellular energy, and defects result in p53 activation via repression of mouse double minute 2 (MDM2) homolog by the ribosomal proteins RPL5 and RPL11. Here, we report that RPL5 and RPL11 regulate p53 from the context of a ribosomal subcomplex, the 5S ribonucleoprotein particle (RNP). We provide evidence that the third component of this complex, the 5S rRNA, is critical for p53 regulation. In addition, we show that the 5S RNP is essential for the activation of p53 by p14ARF, a protein that is activated by oncogene overexpression. Our data show that the abundance of the 5S RNP, and therefore p53 levels, is determined by factors regulating 5S complex formation and ribosome integration, including the tumor suppressor PICT1. The 5S RNP therefore emerges as the critical coordinator of signaling pathways that couple cell proliferation with ribosome production. more...
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- 2013
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3. N 6 ‐Methyladenosine‐Sensitive RNA‐Cleaving Deoxyribozymes
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Maksim V. Sednev, Volodymyr Mykhailiuk, Priyanka Choudhury, Julia Halang, Katherine E. Sloan, Markus T. Bohnsack, and Claudia Höbartner
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0301 basic medicine ,03 medical and health sciences ,030104 developmental biology ,General Medicine ,010402 general chemistry ,01 natural sciences ,0104 chemical sciences - Published
- 2018
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4. The m6A reader protein YTHDC2 interacts with the small ribosomal subunit and the 5′–3′ exoribonuclease XRN1
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Markus T. Bohnsack, Philipp Hackert, Claudia Höbartner, Harita Rao, Jens Kretschmer, and Katherine E. Sloan
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0301 basic medicine ,RNA ,Translation (biology) ,Biology ,Ribosome ,Protein–protein interaction ,Cell biology ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,030220 oncology & carcinogenesis ,Exoribonuclease ,RNA splicing ,Gene expression ,Ankyrin repeat ,Molecular Biology - Abstract
N6-methyladenosine (m6A) modifications in RNAs play important roles in regulating many different aspects of gene expression. While m6As can have direct effects on the structure, maturation, or translation of mRNAs, such modifications can also influence the fate of RNAs via proteins termed “readers” that specifically recognize and bind modified nucleotides. Several YTH domain-containing proteins have been identified as m6A readers that regulate the splicing, translation, or stability of specific mRNAs. In contrast to the other YTH domain-containing proteins, YTHDC2 has several defined domains and here, we have analyzed the contribution of these domains to the RNA and protein interactions of YTHDC2. The YTH domain of YTHDC2 preferentially binds m6A-containing RNAs via a conserved hydrophobic pocket, whereas the ankyrin repeats mediate an RNA-independent interaction with the 5′–3′ exoribonuclease XRN1. We show that the YTH and R3H domains contribute to the binding of YTHDC2 to cellular RNAs, and using crosslinking and analysis of cDNA (CRAC), we reveal that YTHDC2 interacts with the small ribosomal subunit in close proximity to the mRNA entry/exit sites. YTHDC2 was recently found to promote a “fast-track” expression program for specific mRNAs, and our data suggest that YTHDC2 accomplishes this by recruitment of the RNA degradation machinery to regulate the stability of m6A-containing mRNAs and by utilizing its distinct RNA-binding domains to bridge interactions between m6A-containing mRNAs and the ribosomes to facilitate their efficient translation. more...
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- 2018
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5. Unravelling the Mechanisms of RNA Helicase Regulation
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Katherine E. Sloan and Markus T. Bohnsack
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0301 basic medicine ,Coenzymes ,RNA ,Helicase ,Biology ,Biochemistry ,RNA Helicase A ,RNA Helicases ,Cofactor ,Cell biology ,Enzyme Activation ,03 medical and health sciences ,Enzyme activator ,030104 developmental biology ,Gene expression ,Biocatalysis ,biology.protein ,Humans ,Nucleic acid structure ,Protein Processing, Post-Translational ,Molecular Biology - Abstract
RNA helicases are critical regulators at the nexus of multiple pathways of RNA metabolism, and in the complex cellular environment, tight spatial and temporal regulation of their activity is essential. Dedicated protein cofactors play key roles in recruiting helicases to specific substrates and modulating their catalytic activity. Alongside individual RNA helicase cofactors, networks of cofactors containing evolutionarily conserved domains such as the G-patch and MIF4G domains highlight the potential for cross-regulation of different aspects of gene expression. Structural analyses of RNA helicase-cofactor complexes now provide insight into the diverse mechanisms by which cofactors can elicit specific and coordinated regulation of RNA helicase action. Furthermore, post-translational modifications (PTMs) and long non-coding RNA (lncRNA) regulators have recently emerged as novel modes of RNA helicase regulation. more...
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- 2018
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6. <scp>NSUN</scp> 3 and <scp>ABH</scp> 1 modify the wobble position of mt‐t <scp>RNA</scp> Met to expand codon recognition in mitochondrial translation
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Jens Kretschmer, Katherine E. Sloan, Ahmed S. Warda, Namit Ranjan, Charlotte Blessing, Claudia Höbartner, Marina V. Rodnina, Peter Rehling, Sven Dennerlein, Markus T. Bohnsack, Benedikt Hübner, Sara Haag, and Jan Seikowski more...
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0301 basic medicine ,Mitochondrial DNA ,RNA, Transfer, Met ,ABH1 ,mitochondria ,NSUN3 ,RNA modification ,translation ,Mitochondrial translation ,Wobble base pair ,Biology ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,Eukaryotic translation ,Start codon ,Animals ,Humans ,News & Views ,Codon ,Molecular Biology ,Mammals ,Genetics ,General Immunology and Microbiology ,General Neuroscience ,Membrane Proteins ,Methyltransferases ,Sequence Analysis, DNA ,Genetic code ,Stem-loop ,Mitochondria ,030104 developmental biology ,Protein Biosynthesis ,Transfer RNA ,Carboxylic Ester Hydrolases - Abstract
Mitochondrial gene expression uses a non‐universal genetic code in mammals. Besides reading the conventional AUG codon, mitochondrial (mt‐)tRNAMet mediates incorporation of methionine on AUA and AUU codons during translation initiation and on AUA codons during elongation. We show that the RNA methyltransferase NSUN3 localises to mitochondria and interacts with mt‐tRNAMet to methylate cytosine 34 (C34) at the wobble position. NSUN3 specifically recognises the anticodon stem loop (ASL) of the tRNA, explaining why a mutation that compromises ASL basepairing leads to disease. We further identify ALKBH1/ABH1 as the dioxygenase responsible for oxidising m5C34 of mt‐tRNAMet to generate an f5C34 modification. In vitro codon recognition studies with mitochondrial translation factors reveal preferential utilisation of m5C34 mt‐tRNAMet in initiation. Depletion of either NSUN3 or ABH1 strongly affects mitochondrial translation in human cells, implying that modifications generated by both enzymes are necessary for mt‐tRNAMet function. Together, our data reveal how modifications in mt‐tRNAMet are generated by the sequential action of NSUN3 and ABH1, allowing the single mitochondrial tRNAMet to recognise the different codons encoding methionine. ![][1] RNA methyltransferase NSUN3 acts specifically on mitochondrial tRNAMet, allowing different codons to be recognised by this single tRNA and offering insight on the consequence of reported disease mutations. [1]: /embed/graphic-1.gif more...
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- 2016
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7. N
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Maksim V, Sednev, Volodymyr, Mykhailiuk, Priyanka, Choudhury, Julia, Halang, Katherine E, Sloan, Markus T, Bohnsack, and Claudia, Höbartner
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RNA Cleavage ,Adenosine ,Base Sequence ,Nucleic Acid Conformation ,RNA ,DNA, Catalytic ,Methylation ,Substrate Specificity - Abstract
Deoxyribozymes are synthetic enzymes made of DNA that can catalyze the cleavage or formation of phosphodiester bonds and are useful tools for RNA biochemistry. Herein, we report new RNA-cleaving deoxyribozymes to interrogate the methylation status of target RNAs, thereby providing an alternative method for the biochemical validation of RNA methylation sites containing N more...
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- 2018
8. Modifications in small nuclear RNAs and their roles in spliceosome assembly and function
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Katherine E. Sloan and Markus T. Bohnsack
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0301 basic medicine ,Spliceosome ,urogenital system ,Chemistry ,Clinical Biochemistry ,Biochemistry ,RNA Helicase A ,Cell biology ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,030220 oncology & carcinogenesis ,RNA, Small Nuclear ,RNA splicing ,Gene expression ,Spliceosomes ,Humans ,Molecular Biology ,Small nuclear RNA ,SnRNA modification ,Ribonucleoprotein ,SnRNP Biogenesis - Abstract
Modifications in cellular RNAs have emerged as key regulators of all aspects of gene expression, including pre-mRNA splicing. During spliceosome assembly and function, the small nuclear RNAs (snRNAs) form numerous dynamic RNA-RNA and RNA-protein interactions, which are required for spliceosome assembly, correct positioning of the spliceosome on substrate pre-mRNAs and catalysis. The human snRNAs contain several base methylations as well as a myriad of pseudouridines and 2′-O-methylated nucleotides, which are largely introduced by small Cajal body-specific ribonucleoproteins (scaRNPs). Modified nucleotides typically cluster in functionally important regions of the snRNAs, suggesting that their presence could optimise the interactions of snRNAs with each other or with pre-mRNAs, or may affect the binding of spliceosomal proteins. snRNA modifications appear to play important roles in snRNP biogenesis and spliceosome assembly, and have also been proposed to influence the efficiency and fidelity of pre-mRNA splicing. Interestingly, alterations in the modification status of snRNAs have recently been observed in different cellular conditions, implying that some snRNA modifications are dynamic and raising the possibility that these modifications may fine-tune the spliceosome for particular functions. Here, we review the current knowledge on the snRNA modification machinery and discuss the timing, functions and dynamics of modifications in snRNAs. more...
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- 2018
9. RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes
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Henning Urlaub, Markus T. Bohnsack, Lukas Brüning, Jimena Davila Gallesio, Roman Martin, Gerald Ryan R. Aquino, Philipp Hackert, and Katherine E. Sloan
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0301 basic medicine ,Ribosomal Proteins ,Saccharomyces cerevisiae Proteins ,Protein subunit ,Science ,General Physics and Astronomy ,Saccharomyces cerevisiae ,Ribosome ,General Biochemistry, Genetics and Molecular Biology ,Article ,Ribosome assembly ,DEAD-box RNA Helicases ,03 medical and health sciences ,Ribosomal protein ,Ribosome Subunits ,Eukaryotic Small Ribosomal Subunit ,RNA helicases ,pre-ribosomal complexes ,Small nucleolar RNA ,Binding site ,lcsh:Science ,Adenosine Triphosphatases ,Multidisciplinary ,Binding Sites ,Chemistry ,General Chemistry ,Ribosomal RNA ,Cell biology ,030104 developmental biology ,lcsh:Q - Abstract
Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly., Pre-ribosomes undergo numerous structural rearrangements during their assembly. Here the authors identify the binding sites of three essential RNA helicases on pre-ribosomal particles, enabling them to provide insights into the structural and compositional changes that occur during biogenesis of the large ribosomal subunit. more...
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- 2018
10. N 6 -Methyladenosine-Sensitive RNA-Cleaving Deoxyribozymes
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Priyanka Choudhury, Volodymyr Mykhailiuk, Maksim V. Sednev, Katherine E. Sloan, Markus T. Bohnsack, Julia Halang, and Claudia Höbartner
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0301 basic medicine ,RNA methylation ,Deoxyribozyme ,RNA ,General Chemistry ,RNA Biochemistry ,Catalysis ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,chemistry ,Biochemistry ,ddc:540 ,Phosphodiester bond ,Small nucleolar RNA ,N6-Methyladenosine ,DNA - Abstract
Deoxyribozymes are synthetic enzymes made of DNA that can catalyze the cleavage or formation of phosphodiester bonds and are useful tools for RNA biochemistry. Here we report new RNA-cleaving deoxyribozymes to interrogate the methylation status of target RNAs, thereby providing an alternative method for the biochemical validation of RNA methylation sites containing N\(^6\)-methyladenosine, which is the most wide-spread and extensively investigated natural RNA modification. Using in vitro selection from random DNA, we developed deoxyribozymes that are sensitive to the presence of N\(^6\)-methyladenosine in RNA near the cleavage site. One class of these DNA enzymes shows faster cleavage of methylated RNA, while others are strongly inhibited by the modified nucleotide. The general applicability of the new deoxyribozymes is demonstrated for several examples of natural RNA sequences, including a lncRNA and a set of C/D box snoRNAs, which have been suggested to contain m\(^6\)A as a regulatory element that influences RNA folding and protein binding. more...
- Published
- 2018
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11. Human METTL16 is a N6-methyladenosine (m6A) methyltransferase that targets pre-mRNAs and various non-coding RNAs
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Henning Urlaub, Jens Kretschmer, Katherine E. Sloan, Philipp Hackert, Claudia Höbartner, Ahmed S. Warda, Christof Lenz, and Markus T. Bohnsack
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0301 basic medicine ,Genetics ,Methyltransferase ,Biology ,Biochemistry ,Cell biology ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,0302 clinical medicine ,chemistry ,Capping enzyme ,030220 oncology & carcinogenesis ,Gene expression ,RNA splicing ,snRNP ,N6-Methyladenosine ,Molecular Biology ,Biogenesis ,Small nuclear RNA - Abstract
N6-methyladenosine (m6A) is a highly dynamic RNA modification that has recently emerged as a key regulator of gene expression. While many m6A modifications are installed by the METTL3-METTL14 complex, others appear to be introduced independently, implying that additional human m6A methyltransferases remain to be identified. Using crosslinking and analysis of cDNA (CRAC), we reveal that the putative human m6A "writer" protein METTL16 binds to the U6 snRNA and other ncRNAs as well as numerous lncRNAs and pre-mRNAs. We demonstrate that METTL16 is responsible for N6-methylation of A43 of the U6 snRNA and identify the early U6 biogenesis factors La, LARP7 and the methylphosphate capping enzyme MEPCE as METTL16 interaction partners. Interestingly, A43 lies within an essential ACAGAGA box of U6 that base pairs with 5' splice sites of pre-mRNAs during splicing, suggesting that METTL16-mediated modification of this site plays an important role in splicing regulation. The identification of METTL16 as an active m6A methyltransferase in human cells expands our understanding of the mechanisms by which the m6A landscape is installed on cellular RNAs. more...
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- 2017
12. The m
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Jens, Kretschmer, Harita, Rao, Philipp, Hackert, Katherine E, Sloan, Claudia, Höbartner, and Markus T, Bohnsack
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Adenosine Triphosphatases ,Adenosine ,Binding Sites ,Molecular Conformation ,Article ,Ribosome Subunits, Small ,Structure-Activity Relationship ,Exoribonucleases ,Humans ,RNA ,Protein Interaction Domains and Motifs ,Amino Acid Sequence ,Hydrophobic and Hydrophilic Interactions ,Conserved Sequence ,RNA Helicases ,Protein Binding - Abstract
N6-methyladenosine (m6A) modifications in RNAs play important roles in regulating many different aspects of gene expression. While m6As can have direct effects on the structure, maturation, or translation of mRNAs, such modifications can also influence the fate of RNAs via proteins termed “readers” that specifically recognize and bind modified nucleotides. Several YTH domain-containing proteins have been identified as m6A readers that regulate the splicing, translation, or stability of specific mRNAs. In contrast to the other YTH domain-containing proteins, YTHDC2 has several defined domains and here, we have analyzed the contribution of these domains to the RNA and protein interactions of YTHDC2. The YTH domain of YTHDC2 preferentially binds m6A-containing RNAs via a conserved hydrophobic pocket, whereas the ankyrin repeats mediate an RNA-independent interaction with the 5′–3′ exoribonuclease XRN1. We show that the YTH and R3H domains contribute to the binding of YTHDC2 to cellular RNAs, and using crosslinking and analysis of cDNA (CRAC), we reveal that YTHDC2 interacts with the small ribosomal subunit in close proximity to the mRNA entry/exit sites. YTHDC2 was recently found to promote a “fast-track” expression program for specific mRNAs, and our data suggest that YTHDC2 accomplishes this by recruitment of the RNA degradation machinery to regulate the stability of m6A-containing mRNAs and by utilizing its distinct RNA-binding domains to bridge interactions between m6A-containing mRNAs and the ribosomes to facilitate their efficient translation. more...
- Published
- 2017
13. Human METTL16 is a
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Ahmed S, Warda, Jens, Kretschmer, Philipp, Hackert, Christof, Lenz, Henning, Urlaub, Claudia, Höbartner, Katherine E, Sloan, and Markus T, Bohnsack
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Adenosine ,DNA, Complementary ,Base Sequence ,RNA Splicing ,Recombinant Fusion Proteins ,Green Fluorescent Proteins ,Scientific Reports ,Methyltransferases ,Methylation ,HEK293 Cells ,Ribonucleoproteins ,RNA, Small Nuclear ,RNA Precursors ,Humans ,RNA, Long Noncoding ,RNA, Messenger ,Base Pairing ,Oligopeptides ,HeLa Cells - Abstract
N 6‐methyladenosine (m6A) is a highly dynamic RNA modification that has recently emerged as a key regulator of gene expression. While many m6A modifications are installed by the METTL3–METTL14 complex, others appear to be introduced independently, implying that additional human m6A methyltransferases remain to be identified. Using crosslinking and analysis of cDNA (CRAC), we reveal that the putative human m6A “writer” protein METTL16 binds to the U6 snRNA and other ncRNAs as well as numerous lncRNAs and pre‐mRNAs. We demonstrate that METTL16 is responsible for N 6‐methylation of A43 of the U6 snRNA and identify the early U6 biogenesis factors La, LARP7 and the methylphosphate capping enzyme MEPCE as METTL16 interaction partners. Interestingly, A43 lies within an essential ACAGAGA box of U6 that base pairs with 5′ splice sites of pre‐mRNAs during splicing, suggesting that METTL16‐mediated modification of this site plays an important role in splicing regulation. The identification of METTL16 as an active m6A methyltransferase in human cells expands our understanding of the mechanisms by which the m6A landscape is installed on cellular RNAs. more...
- Published
- 2017
14. Crosslinking Methods to Identify RNA Methyltransferase Targets In Vivo
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Sara, Haag, Jens, Kretschmer, Katherine E, Sloan, and Markus T, Bohnsack
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Ultraviolet Rays ,Statistics as Topic ,Azacitidine ,Computational Biology ,High-Throughput Nucleotide Sequencing ,RNA ,Cytidine ,Methyltransferases ,Chromatography, Affinity ,Substrate Specificity - Abstract
Several crosslinking methods have been developed to identify interacting RNAs for proteins of interest. Here, we describe variants of the UV crosslinking and analysis of cDNA (CRAC) method that allow target identification of RNA methyltransferases on a genome-wide scale. We present a detailed protocol for the application of CRAC in human cells that stably express the protein of interest fused to a tandem affinity tag. After the introduction of a covalent link between the protein and its target RNAs, protein-RNA complexes are purified and bound RNAs trimmed, ligated to adapters, reverse transcribed, and amplified. Sequences obtained from next-generation sequencing are then mapped onto the human genome allowing the identification of possible substrates. For some RNA methyltransferases, e.g., m more...
- Published
- 2017
15. In Vitro Assays for RNA Methyltransferase Activity
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Sara, Haag, Katherine E, Sloan, Claudia, Höbartner, and Markus T, Bohnsack
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Enzyme Activation ,Epigenomics ,RNA ,Methyltransferases ,In Vitro Techniques ,Methylation ,Chromatography, High Pressure Liquid ,Enzyme Assays ,Epigenesis, Genetic ,Substrate Specificity - Abstract
RNA methyltransferases (MTases) are responsible for co- and posttranscriptional methylation of nucleotides in a wide variety of RNA substrates. Examination of the target specificity, catalytic activity, and function of these enzymes requires in vitro methylation assays. Here, we provide a detailed protocol for the methylation of in vitro transcripts, synthetic RNAs, and total cellular RNA using recombinant RNA methyltransferases and S-adenosylmethionine (SAM) as a methyl group donor. We describe how this method can be coupled to fluorographic detection of RNA methylation if more...
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- 2017
16. Crosslinking Methods to Identify RNA Methyltransferase Targets In Vivo
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Sara Haag, Markus T. Bohnsack, Jens Kretschmer, and Katherine E. Sloan
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0301 basic medicine ,Methyltransferase ,030102 biochemistry & molecular biology ,RNA ,macromolecular substances ,03 medical and health sciences ,5-Methylcytosine ,chemistry.chemical_compound ,030104 developmental biology ,chemistry ,Biochemistry ,In vivo ,Covalent bond ,Complementary DNA ,Human genome - Abstract
Several crosslinking methods have been developed to identify interacting RNAs for proteins of interest. Here, we describe variants of the UV crosslinking and analysis of cDNA (CRAC) method that allow target identification of RNA methyltransferases on a genome-wide scale. We present a detailed protocol for the application of CRAC in human cells that stably express the protein of interest fused to a tandem affinity tag. After the introduction of a covalent link between the protein and its target RNAs, protein-RNA complexes are purified and bound RNAs trimmed, ligated to adapters, reverse transcribed, and amplified. Sequences obtained from next-generation sequencing are then mapped onto the human genome allowing the identification of possible substrates. For some RNA methyltransferases, e.g., m5C MTases, their catalytic mechanism can be exploited for chemical crosslinking approaches instead of UV based crosslinking. more...
- Published
- 2017
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17. Tuning the ribosome: the influence of rRNA modification on eukaryotic ribosome biogenesis and function
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Markus T. Bohnsack, Ahmed S. Warda, Sunny Sharma, Katherine E. Sloan, Denis L. J. Lafontaine, and Karl-Dieter Entian
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0301 basic medicine ,RNA, Ribosomal -- chemistry -- genetics -- metabolism ,5.8S ribosomal RNA ,translation ,Review ,Biology ,ribosomopathy ,snoRNA ,Ribosome ,Methylation ,RNA methyltransferase ,RNA modification ,acetylation ,methylation ,pseudouridylation ,ribosome ,Eukaryotic Cells -- physiology ,03 medical and health sciences ,Structure-Activity Relationship ,RRNA modification ,23S ribosomal RNA ,RNA, Small Nucleolar ,Animals ,Humans ,Ribosome profiling ,Molecular Biology ,RNA, Small Nucleolar -- genetics -- metabolism ,Genetics ,Acetylation ,Cell Biology ,Ribosomal RNA ,Sciences bio-médicales et agricoles ,Cell biology ,Ribosomes -- chemistry -- metabolism ,Internal ribosome entry site ,Eukaryotic Cells ,030104 developmental biology ,RNA, Ribosomal ,Disease Susceptibility ,Eukaryotic Ribosome ,Ribosomes - Abstract
rRNAs are extensively modified during their transcription and subsequent maturation in the nucleolus, nucleus and cytoplasm. RNA modifications, which are installed either by snoRNA-guided or by stand-alone enzymes, generally stabilize the structure of the ribosome. However, they also cluster at functionally important sites of the ribosome, such as the peptidyltransferase center and the decoding site, where they facilitate efficient and accurate protein synthesis. The recent identification of sites of substoichiometric 2'-O-methylation and pseudouridylation has overturned the notion that all rRNA modifications are constitutively present on ribosomes, highlighting nucleotide modifications as an important source of ribosomal heterogeneity. While the mechanisms regulating partial modification and the functions of specialized ribosomes are largely unknown, changes in the rRNA modification pattern have been observed in response to environmental changes, during development, and in disease. This suggests that rRNA modifications may contribute to the translational control of gene expression., SCOPUS: re.j, info:eu-repo/semantics/published more...
- Published
- 2017
18. Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways
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Dagmar Klostermeier, Katherine E. Sloan, Mira Prior, Henning Urlaub, Philipp Hackert, Jörg Enderlein, Annika U. Heininger, Reinhard Lührmann, Markus Deckers, Indira Memet, Markus T. Bohnsack, Bernhard Schmidt, Peter Rehling, Kum-Loong Boon, Enrico Schleiff, Anne Clancy, and Alexandra Z. Andreou more...
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0301 basic medicine ,Cytoplasm ,Saccharomyces cerevisiae Proteins ,RNA helicase ,G-patch protein ,ribosome ,splicing ,protein cofactor ,Ribosome biogenesis ,Apoptosis ,Saccharomyces cerevisiae ,Biology ,Ribosome ,DEAD-box RNA Helicases ,03 medical and health sciences ,Gene Expression Regulation, Fungal ,medicine ,Molecular Biology ,Cellular localization ,Cell Nucleus ,Helicase ,RNA ,Cell Biology ,RNA Helicase A ,Molecular biology ,Cell biology ,Cell nucleus ,030104 developmental biology ,medicine.anatomical_structure ,Mitochondrial Membranes ,RNA splicing ,biology.protein ,Signal Transduction ,Research Paper - Abstract
A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes. Open-Access Publikationsfonds 2016 peerReviewed more...
- Published
- 2016
19. Comparison of the yeast and human nuclear exosome complexes
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Nicholas J. Watkins, Claudia Schneider, and Katherine E. Sloan
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Saccharomyces cerevisiae Proteins ,Multiprotein complex ,Polyadenylation ,biology ,RNA Stability ,Saccharomyces cerevisiae ,RNA ,RNA surveillance ,Exosomes ,biology.organism_classification ,Biochemistry ,Exosome ,Molecular biology ,Cell biology ,TRAMP complex ,Humans ,RNA Processing, Post-Transcriptional ,Function (biology) - Abstract
Most RNAs in eukaryotic cells are produced as precursors that undergo processing at the 3′ and/or 5′ end to generate the mature transcript. In addition, many transcripts are degraded not only as part of normal recycling, but also when recognized as aberrant by the RNA surveillance machinery. The exosome, a conserved multiprotein complex containing two nucleases, is involved in both the 3′ processing and the turnover of many RNAs in the cell. A series of factors, including the TRAMP (Trf4–Air2–Mtr4 polyadenylation) complex, Mpp6 and Rrp47, help to define the targets to be processed and/or degraded and assist in exosome function. The majority of the data on the exosome and RNA maturation/decay have been derived from work performed in the yeast Saccharomyces cerevisiae. In the present paper, we provide an overview of the exosome and its role in RNA processing/degradation and discuss important new insights into exosome composition and function in human cells. more...
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- 2012
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20. Box C/D snoRNP catalysed methylation is aided by additional pre-rRNA base-pairing
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Katherine E. Sloan, Sander Granneman, David Tollervey, Rob W. van Nues, Nicholas J. Watkins, Grzegorz Kudla, and Matthew Chicken
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Genetics ,0303 health sciences ,General Immunology and Microbiology ,urogenital system ,General Neuroscience ,030302 biochemistry & molecular biology ,RNA ,RRNA methylation ,RRNA binding ,Ribosomal RNA ,Biology ,Ribosome ,General Biochemistry, Genetics and Molecular Biology ,Conserved sequence ,03 medical and health sciences ,RRNA modification ,Biochemistry ,Small nucleolar RNA ,Molecular Biology ,030304 developmental biology - Abstract
2′-O-methylation of eukaryotic ribosomal RNA (r)RNA, essential for ribosome function, is catalysed by box C/D small nucleolar (sno)RNPs. The RNA components of these complexes (snoRNAs) contain one or two guide sequences, which, through base-pairing, select the rRNA modification site. Adjacent to the guide sequences are protein-binding sites (the C/D or C′/D′ motifs). Analysis of >2000 yeast box C/D snoRNAs identified additional conserved sequences in many snoRNAs that are complementary to regions adjacent to the rRNA methylation site. This ‘extra base-pairing' was also found in many human box C/D snoRNAs and can stimulate methylation by up to five-fold. Sequence analysis, combined with RNA–protein crosslinking in Saccharomyces cerevisiae, identified highly divergent box C′/D′ motifs that are bound by snoRNP proteins. In vivo rRNA methylation assays showed these to be active. Our data suggest roles for non-catalytic subunits (Nop56 and Nop58) in rRNA binding and support an asymmetric model for box C/D snoRNP organization. The study provides novel insights into the extent of the snoRNA–rRNA interactions required for efficient methylation and the structural organization of the snoRNPs. more...
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- 2011
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21. Cover Picture: N 6 ‐Methyladenosine‐Sensitive RNA‐Cleaving Deoxyribozymes (Angew. Chem. Int. Ed. 46/2018)
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Priyanka Choudhury, Volodymyr Mykhailiuk, Markus T. Bohnsack, Katherine E. Sloan, Claudia Höbartner, Maksim V. Sednev, and Julia Halang
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010405 organic chemistry ,Chemistry ,Stereochemistry ,INT ,Deoxyribozyme ,RNA ,General Chemistry ,01 natural sciences ,Catalysis ,0104 chemical sciences ,chemistry.chemical_compound ,RNA modification ,Cover (algebra) ,N6-Methyladenosine - Published
- 2018
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22. Nucleocytoplasmic Transport of RNAs and RNA-Protein Complexes
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Katherine E. Sloan, Pierre-Emmanuel Gleizes, and Markus T. Bohnsack
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0301 basic medicine ,Cytoplasm ,Active Transport, Cell Nucleus ,RNA ,Nuclear Proteins ,Biology ,Cell biology ,Nuclear Pore Complex Proteins ,03 medical and health sciences ,030104 developmental biology ,Structural Biology ,Nucleocytoplasmic Transport ,Gene expression ,Nuclear Pore ,Humans ,Nucleoporin ,Nuclear pore ,Nuclear transport ,Nuclear protein ,Molecular Biology ,Ribonucleoprotein - Abstract
RNAs and ribonucleoprotein complexes (RNPs) play key roles in mediating and regulating gene expression. In eukaryotes, most RNAs are transcribed, processed and assembled with proteins in the nucleus and then either function in the cytoplasm or also undergo a cytoplasmic phase in their biogenesis. This compartmentalization ensures that sequential steps in gene expression and RNP production are performed in the correct order and it allows important quality control mechanisms that prevent the involvement of aberrant RNAs/RNPs in these cellular pathways. The selective exchange of RNAs/RNPs between the nucleus and cytoplasm is enabled by nuclear pore complexes, which function as gateways between these compartments. RNA/RNP transport is facilitated by a range of nuclear transport receptors and adaptors, which are specifically recruited to their cargos and mediate interactions with nucleoporins to allow directional translocation through nuclear pore complexes. While some transport factors are only responsible for the export/import of a certain class of RNA/RNP, others are multifunctional and, in the case of large RNPs, several export factors appear to work together to bring about export. Recent structural studies have revealed aspects of the mechanisms employed by transport receptors to enable specific cargo recognition, and genome-wide approaches have provided the first insights into the diverse composition of pre-mRNPs during export. Furthermore, the regulation of RNA/RNP export is emerging as an important means to modulate gene expression under stress conditions and in disease. more...
- Published
- 2015
23. Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways
- Author
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Annika U. Heininger, Philipp Hackert, Alexandra Z. Andreou, Kum-Loong Boon, Indira Memet, Mira Prior, Anne Clancy, Bernhard Schmidt, Henning Urlaub, Enrico Schleiff, Katherine E. Sloan, Markus Deckers, Reinhard Lührmann, Jörg Enderlein, Dagmar Klostermeier, Peter Rehling, Markus T. Bohnsack, Annika U. Heininger, Philipp Hackert, Alexandra Z. Andreou, Kum-Loong Boon, Indira Memet, Mira Prior, Anne Clancy, Bernhard Schmidt, Henning Urlaub, Enrico Schleiff, Katherine E. Sloan, Markus Deckers, Reinhard Lührmann, Jörg Enderlein, Dagmar Klostermeier, Peter Rehling, and Markus T. Bohnsack more...
- Published
- 2016
- Full Text
- View/download PDF
24. Corrigendum: A novel translational control mechanism involving RNA structures within coding sequences
- Author
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Sebastian A. Leidel, Neus Martínez-Bosch, Pilar Navarro, Emanuele Raineri, Danny D. Nedialkova, Katherine E. Sloan, Lukas Brüning, Juana Díez, Markus T. Bohnsack, Jennifer Jungfleisch, and Ivan Dotu
- Subjects
0301 basic medicine ,Saccharomyces cerevisiae Proteins ,Saccharomyces cerevisiae ,Computational biology ,Biology ,Bioinformatics ,DEAD-box RNA Helicases ,Open Reading Frames ,03 medical and health sciences ,Text mining ,Genetics ,Humans ,RNA, Messenger ,Peptide Chain Initiation, Translational ,Control (linguistics) ,Genetics (clinical) ,Mechanism (biology) ,business.industry ,Research ,RNA ,Exons ,Bromovirus ,030104 developmental biology ,Gene Expression Regulation ,Protein Biosynthesis ,Nucleic Acid Conformation ,Corrigendum ,business ,Ribosomes ,Coding (social sciences) - Abstract
The impact of RNA structures in coding sequences (CDS) within mRNAs is poorly understood. Here, we identify a novel and highly conserved mechanism of translational control involving RNA structures within coding sequences and the DEAD-box helicase Dhh1. Using yeast genetics and genome-wide ribosome profiling analyses, we show that this mechanism, initially derived from studies of the Brome Mosaic virus RNA genome, extends to yeast and human mRNAs highly enriched in membrane and secreted proteins. All Dhh1-dependent mRNAs, viral and cellular, share key common features. First, they contain long and highly structured CDSs, including a region located around nucleotide 70 after the translation initiation site; second, they are directly bound by Dhh1 with a specific binding distribution; and third, complementary experimental approaches suggest that they are activated by Dhh1 at the translation initiation step. Our results show that ribosome translocation is not the only unwinding force of CDS and uncover a novel layer of translational control that involves RNA helicases and RNA folding within CDS providing novel opportunities for regulation of membrane and secretome proteins. more...
- Published
- 2017
- Full Text
- View/download PDF
25. A pre-ribosomal RNA interaction network involving snoRNAs and the Rok1 helicase
- Author
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Maike Ruprecht, Oliver Mirus, Markus T. Bohnsack, Enrico Schleiff, Stefan Simm, Philipp Hackert, Grzegorz Kudla, Lukas Brüning, Katherine E. Sloan, and Roman Martin
- Subjects
Genetics ,Saccharomyces cerevisiae Proteins ,5.8S ribosomal RNA ,Ribosome biogenesis ,macromolecular substances ,Saccharomyces cerevisiae ,Ribosomal RNA ,Biology ,Non-coding RNA ,Ribosome ,Cell biology ,DEAD-box RNA Helicases ,A-site ,RNA, Ribosomal ,Report ,ddc:570 ,TRAMP complex ,RNA Precursors ,RNA, Ribosomal, 18S ,Nucleic Acid Conformation ,RNA, Small Nucleolar ,Small nucleolar RNA ,Base Pairing ,Molecular Biology ,Protein Binding - Abstract
Ribosome biogenesis in yeast requires 75 small nucleolar RNAs (snoRNAs) and a myriad of cofactors for processing, modification, and folding of the ribosomal RNAs (rRNAs). For the 19 RNA helicases implicated in ribosome synthesis, their sites of action and molecular functions have largely remained unknown. Here, we have used UV cross-linking and analysis of cDNA (CRAC) to reveal the pre-rRNA binding sites of the RNA helicase Rok1, which is involved in early small subunit biogenesis. Several contact sites were identified in the 18S rRNA sequence, which interestingly all cluster in the “foot” region of the small ribosomal subunit. These include a major binding site in the eukaryotic expansion segment ES6, where Rok1 is required for release of the snR30 snoRNA. Rok1 directly contacts snR30 and other snoRNAs required for pre-rRNA processing. Using cross-linking, ligation and sequencing of hybrids (CLASH) we identified several novel pre-rRNA base-pairing sites for the snoRNAs snR30, snR10, U3, and U14, which cluster in the expansion segments of the 18S rRNA. Our data suggest that these snoRNAs bridge interactions between the expansion segments, thereby forming an extensive interaction network that likely promotes pre-rRNA maturation and folding in early pre-ribosomal complexes and establishes long-range rRNA interactions during ribosome synthesis. more...
- Published
- 2014
- Full Text
- View/download PDF
26. The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA
- Author
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Katherine E, Sloan, Markus T, Bohnsack, Claudia, Schneider, and Nicholas J, Watkins
- Subjects
Reverse Transcriptase Polymerase Chain Reaction ,Articles ,Blotting, Northern ,Exosomes ,Real-Time Polymerase Chain Reaction ,Ribosome Subunits, Small ,HEK293 Cells ,RNA, Ribosomal ,Ribonucleoproteins, Small Nucleolar ,Exoribonucleases ,MCF-7 Cells ,RNA Precursors ,Humans ,RNA, Messenger ,RNA Processing, Post-Transcriptional ,RNA Helicases ,HeLa Cells - Abstract
During eukaryotic ribosome biogenesis, three of the mature ribosomal (r)RNAs are released from a single precursor transcript (pre-rRNA) by an ordered series of endonucleolytic cleavages and exonucleolytic processing steps. Production of the 18S rRNA requires the removal of the 5' external transcribed spacer (5'ETS) by endonucleolytic cleavages at sites A0 and A1/site 1. In metazoans, an additional cleavage in the 5'ETS, at site A', upstream of A0, has also been reported. Here, we have investigated how A' processing is coordinated with assembly of the early preribosomal complex. We find that only the tUTP (UTP-A) complex is critical for A' cleavage, while components of the bUTP (UTP-B) and U3 snoRNP are important, but not essential, for efficient processing at this site. All other factors involved in the early stages of 18S rRNA processing that were tested here function downstream from this processing step. Interestingly, we show that the RNA surveillance factors XRN2 and MTR4 are also involved in A' cleavage in humans. A' cleavage is largely bypassed when XRN2 is depleted, and we also discover that A' cleavage is not always the initial processing event in all cell types. Together, our data suggest that A' cleavage is not a prerequisite for downstream pre-rRNA processing steps and may, in fact, represent a quality control step for initial pre-rRNA transcripts. Furthermore, we show that components of the RNA surveillance machinery, including the exosome and TRAMP complexes, also play key roles in the recycling of excised spacer fragments and degradation of aberrant pre-rRNAs in human cells. more...
- Published
- 2014
27. Both endonucleolytic and exonucleolytic cleavage mediate ITS1 removal during human ribosomal RNA processing
- Author
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Ger J. M. Pruijn, Sandy Mattijssen, Nicholas J. Watkins, Katherine E. Sloan, David Tollervey, and Simon Lebaron
- Subjects
Enzyme complex ,Saccharomyces cerevisiae Proteins ,Endoribonuclease ,5.8S ribosomal RNA ,RNA-binding protein ,Saccharomyces cerevisiae ,Biology ,Transfection ,Ribosome ,Article ,03 medical and health sciences ,0302 clinical medicine ,Endoribonucleases ,RNA Precursors ,RNA, Ribosomal, 18S ,Humans ,RNA Processing, Post-Transcriptional ,GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries) ,Research Articles ,030304 developmental biology ,Genetics ,0303 health sciences ,Exosome Multienzyme Ribonuclease Complex ,Bio-Molecular Chemistry ,RNA ,Proteins ,RNA-Binding Proteins ,RNA, Fungal ,Cell Biology ,Ribosomal RNA ,3. Good health ,Cell biology ,HEK293 Cells ,RNA, Ribosomal ,Exoribonucleases ,RNA Interference ,Ribosomes ,030217 neurology & neurosurgery ,HeLa Cells - Abstract
Human ribosomal RNA processing is initiated by endonuclease cleavage and followed by 3′ to 5′ exonucleolytic processing by RRP6 and the exosome., Human ribosome production is up-regulated during tumorogenesis and is defective in many genetic diseases (ribosomopathies). We have undertaken a detailed analysis of human precursor ribosomal RNA (pre-rRNA) processing because surprisingly little is known about this important pathway. Processing in internal transcribed spacer 1 (ITS1) is a key step that separates the rRNA components of the large and small ribosomal subunits. We report that this was initiated by endonuclease cleavage, which required large subunit biogenesis factors. This was followed by 3′ to 5′ exonucleolytic processing by RRP6 and the exosome, an enzyme complex not previously linked to ITS1 removal. In contrast, RNA interference–mediated knockdown of the endoribonuclease MRP did not result in a clear defect in ITS1 processing. Despite the apparently high evolutionary conservation of the pre-rRNA processing pathway and ribosome synthesis factors, each of these features of human ITS1 processing is distinct from those in budding yeast. These results also provide significant insight into the links between ribosomopathies and ribosome production in human cells. more...
- Published
- 2013
- Full Text
- View/download PDF
28. Effects of the Bowen-Conradi syndrome mutation in EMG1 on its nuclear import, stability and nucleolar recruitment
- Author
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Sara Haag, Markus T. Bohnsack, Bernard Freytag, Katherine E. Sloan, Dirk Görlich, and Ahmed S. Warda
- Subjects
0301 basic medicine ,Nucleolus ,Active Transport, Cell Nucleus ,Importin ,Biology ,Ribosome ,03 medical and health sciences ,RNA, Ribosomal, 18S ,Genetics ,medicine ,Humans ,Nuclear protein ,Molecular Biology ,Genetics (clinical) ,Fetal Growth Retardation ,Nuclear Proteins ,RNA ,Articles ,Methyltransferases ,General Medicine ,Ribosomal RNA ,beta Karyopherins ,Molecular biology ,Cell nucleus ,030104 developmental biology ,medicine.anatomical_structure ,Multiprotein Complexes ,Mutation ,Psychomotor Disorders ,Nuclear transport ,Cell Nucleolus ,HeLa Cells ,Protein Binding - Abstract
Bowen-Conradi syndrome (BCS) is a severe genetic disorder that is characterised by various developmental abnormalities, bone marrow failure and early infant death. This disease is caused by a single mutation leading to the aspartate 86 to glycine (D86G) exchange in the essential nucleolar RNA methyltransferase EMG1. EMG1 is required for the synthesis of the small ribosomal subunit and is involved in modification of the 18S ribosomal RNA. Here, we identify the pre-ribosomal factors NOP14, NOC4L and UTP14A as members of a nucleolar subcomplex that contains EMG1 and is required for its recruitment to nucleoli. The BCS mutation in EMG1 leads to reduced nucleolar localisation, accumulation of EMG1(D86G) in nuclear foci and its proteasome-dependent degradation. We further show that EMG1 can be imported into the nucleus by the importins (Imp) Imp alpha/beta or Imp beta/7. Interestingly, in addition to its role in nuclear import, binding of the Imp beta/7 heterodimer can prevent unspecific aggregation of both EMG1 and EMG1(D86G) on RNAs in vitro, indicating that the importins act as chaperones by binding to basic regions of the RNA methyltransferase. Our findings further indicate that in BCS, nuclear disassembly of the import complex and release of EMG1(D86G) lead to its nuclear aggregation and degradation, resulting in the reduced nucleolar recruitment of the RNA methyltransferase and defects in the biogenesis of the small ribosomal subunit. more...
- Published
- 2016
- Full Text
- View/download PDF
29. The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans
- Author
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Katherine E. Sloan, Graeme R. Wells, David Tollervey, David Colvin, Nicholas J. Watkins, Franziska Weichmann, Claudia Schneider, and Grzegorz Kudla
- Subjects
0301 basic medicine ,03 medical and health sciences ,Endonuclease ,030104 developmental biology ,Biochemistry ,biology ,Genetics ,biology.protein ,RNA ,Ribosomal RNA ,Corrigendum ,PIN domain ,Yeast - Abstract
During ribosomal RNA (rRNA) maturation, cleavages at defined sites separate the mature rRNAs from spacer regions, but the identities of several enzymes required for 18S rRNA release remain unknown. PilT N-terminus (PIN) domain proteins are frequently endonucleases and the PIN domain protein Utp24 is essential for early cleavages at three pre-rRNA sites in yeast (A0, A1 and A2) and humans (A0, 1 and 2a). In yeast, A1 is cleaved prior to A2 and both cleavages require base-pairing by the U3 snoRNA to the central pseudoknot elements of the 18S rRNA. We found that yeast Utp24 UV-crosslinked in vivo to U3 and the pseudoknot, placing Utp24 close to cleavage at site A1. Yeast and human Utp24 proteins exhibited in vitro endonuclease activity on an RNA substrate containing yeast site A2. Moreover, an intact PIN domain in human UTP24 was required for accurate cleavages at sites 1 and 2a in vivo, whereas mutation of another potential site 2a endonuclease, RCL1, did not affect 18S production. We propose that Utp24 cleaves sites A1/1 and A2/2a in yeast and human cells. more...
- Published
- 2016
- Full Text
- View/download PDF
30. A novel translational control mechanism involving RNA structures within coding sequences
- Author
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Lukas Brüning, Juana Díez, Sebastian A. Leidel, Neus Martínez-Bosch, Jennifer Jungfleisch, Markus T. Bohnsack, Ivan Dotu, Danny D. Nedialkova, Katherine E. Sloan, Pilar Navarro, and Emanuele Raineri
- Subjects
0301 basic medicine ,biology ,Helicase ,RNA ,Computational biology ,biology.organism_classification ,Ribosome ,Genome ,3. Good health ,03 medical and health sciences ,030104 developmental biology ,0302 clinical medicine ,Eukaryotic translation ,Brome mosaic virus ,030220 oncology & carcinogenesis ,Genetics ,biology.protein ,Protein biosynthesis ,Ribosome profiling ,Genomes ,Genetics (clinical) ,Genètica - Abstract
The impact of RNA structures in coding sequences (CDS) within mRNAs is poorly understood. Here, we identify a novel and highly conserved mechanism of translational control involving RNA structures within coding sequences and the DEAD-box helicase Dhh1. Using yeast genetics and genome-wide ribosome profiling analyses, we show that this mechanism, initially derived from studies of the Brome Mosaic virus RNA genome, extends to yeast and human mRNAs highly enriched in membrane and secreted proteins. All Dhh1-dependent mRNAs, viral and cellular, share key common features. First, they contain long and highly structured CDSs, including a region located around nucleotide 70 after the translation initiation site; second, they are directly bound by Dhh1 with a specific binding distribution; and third, complementary experimental approaches suggest that they are activated by Dhh1 at the translation initiation step. Our results show that ribosome translocation is not the only unwinding force of CDS and uncover a novel layer of translational control that involves RNA helicases and RNA folding within CDS providing novel opportunities for regulation of membrane and secretome proteins. This work was supported by the Spanish Ministry of Economy and Competitiveness through grant BFU 2013-44629-R and the “Maria de Maeztu” Programme for Units of Excellence in R&D (MDM-2014-0370). J.J. was supported by the grant 2012FI_B00574 from the Generalitat de Catalunya. This work was also supported by the Deutsche Forschungsgemeinschaft/n(SFB860 to M.T.B.), the Alexander von Humboldt foundation/n(to K.E.S. and M.T.B.), the Max Planck Society (to S.A.L.),/nthe Spanish Ministerio de Economia y Competividad/ISCIIIFEDER/n(PI14/00125 to P.N.), and the Generalitat de Catalunya/n(2014/SGR/143 to P.N.) more...
31. How RNA modification allows non-conventional decoding in mitochondria
- Author
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Markus T. Bohnsack, Claudia Höbartner, and Katherine E. Sloan
- Subjects
0301 basic medicine ,Methyltransferase ,RNA ,Translation (biology) ,Cell Biology ,Mitochondrion ,Biology ,Editorials: Cell Cycle Features ,Models, Biological ,Mitochondria ,03 medical and health sciences ,5-Methylcytosine ,chemistry.chemical_compound ,030104 developmental biology ,Biochemistry ,chemistry ,RNA, Transfer ,Organelle ,Transfer RNA ,Anticodon ,Humans ,Molecular Biology ,Gene ,Developmental Biology - Abstract
Mitochondria are organelles of symbiotic origin that have retained a gene expression machinery during evolution. However, the large majority of the genes encoding mitochondrial proteins have been t... more...
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