9 results on '"Andrea Barta"'
Search Results
2. Organelle Remote Control of Alternative Splicing Through TOR
- Author
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Maria Kalyna, Andrea Barta, Christian Meyer, Alberto R. Kornblihtt, Lucas Servi, Stefan Riegler, Armin Fuchs, and Ezequiel Petrillo
- Subjects
Chloroplast ,Organelle ,Alternative splicing ,Gene expression ,Regulator ,Translation (biology) ,Signal transduction ,Mitochondrion ,Biology ,Cell biology - Abstract
Light makes the difference between life and death for plants, it is their source of energy and also a regulator of plant growth and adaptations to the environment. In plants, light regulates gene expression at various levels including alternative splicing. Chloroplasts are a key part in this process sensing light and providing retrograde signals which modulate alternative splicing in the leaves but also in the roots. We show here that sugars are the mobile signals responsible for the alternative splicing changes in the roots. We provide evidence for the involvement of mitochondria and the activation of TOR kinase in this light signaling pathway. Furthermore, translation activation seems to be of most relevance in order to properly adjust the alternative splicing patterns in response to light/dark transitions and might be a common node for cross-regulation by different pathways.
- Published
- 2018
3. Alternative splicing in plants – coming of age
- Author
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Maria Kalyna, Naeem H. Syed, Andrea Barta, John W. S. Brown, and Yamile Marquez
- Subjects
0106 biological sciences ,Transcription, Genetic ,Nonsense-mediated decay ,Circadian clock ,Review ,Plant Science ,Biology ,Genes, Plant ,01 natural sciences ,Epigenesis, Genetic ,Evolution, Molecular ,Polyploidy ,03 medical and health sciences ,Gene Expression Regulation, Plant ,Circadian Clocks ,Gene expression ,RNA, Messenger ,Gene ,Plant Proteins ,030304 developmental biology ,2. Zero hunger ,Regulation of gene expression ,Genetics ,0303 health sciences ,Protein Stability ,fungi ,Alternative splicing ,food and beverages ,Plants ,Phenotype ,Nonsense Mediated mRNA Decay ,Alternative Splicing ,RNA, Plant ,Evolutionary biology ,Adaptation ,010606 plant biology & botany - Abstract
More than 60% of intron-containing genes undergo alternative splicing (AS) in plants. This number will increase when AS in different tissues, developmental stages, and environmental conditions are explored. Although the functional impact of AS on protein complexity is still understudied in plants, recent examples demonstrate its importance in regulating plant processes. AS also regulates transcript levels and the link with nonsense-mediated decay and generation of unproductive mRNAs illustrate the need for both transcriptional and AS data in gene expression analyses. AS has influenced the evolution of the complex networks of regulation of gene expression and variation in AS contributed to adaptation of plants to their environment and therefore will impact strategies for improving plant and crop phenotypes.
- Published
- 2012
- Full Text
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4. Co-localisation studies of Arabidopsis SR splicing factors reveal different types of speckles in plant cell nuclei
- Author
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Julia Hilscher, Zdravko J. Lorković, and Andrea Barta
- Subjects
Cell type ,RNA Splicing ,Recombinant Fusion Proteins ,Arabidopsis ,Biology ,Ribonucleoprotein, U1 Small Nuclear ,SR protein ,Transcription (biology) ,Two-Hybrid System Techniques ,Tobacco ,Animals ,Humans ,Gene ,Cell Nucleus ,Serine-Arginine Splicing Factors ,Arabidopsis Proteins ,Protoplasts ,Alternative splicing ,RNA-Binding Proteins ,Cell Biology ,biology.organism_classification ,Plant cell ,Molecular biology ,Cell biology ,RNA splicing - Abstract
SR proteins are multidomain splicing factors which are important for spliceosome assembly and for regulation of alternative splicing. In mammalian nuclei these proteins localise to speckles from where they are recruited to transcription sites. By using fluorescent protein fusion technology and different experimental approaches it has been shown that Arabidopsis SR proteins, in addition to diffuse nucleoplasmic staining, localise into an irregular nucleoplasmic network resembling speckles in mammalian cells. As Arabidopsis SR proteins fall into seven conserved sub-families we investigated co-localisation of members of the different sub-families in transiently transformed tobacco protoplast. Here we demonstrate the new finding that members of different SR protein sub-families localise into distinct populations of nuclear speckles with no, partial or complete co-localisation. This is particularly interesting as we also show that these proteins do interact in a yeast two-hybrid assay as well as in pull-down and in co-immunopreciptiation assays. Our data raise the interesting possibility that SR proteins are partitioned into distinct populations of nuclear speckles to allow a more specific recruitment to the transcription/pre-mRNA processing sites of particular genes depending on cell type and developmental stage.
- Published
- 2008
5. Compartmentalization of the splicing machinery in plant cell nuclei
- Author
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Zdravko J. Lorković and Andrea Barta
- Subjects
Cell Nucleus ,Genetics ,Transcription, Genetic ,food and beverages ,Plant Science ,Plants ,Biology ,Compartmentalization (psychology) ,Cell Compartmentation ,Chromatin ,Cell biology ,Alternative Splicing ,Cell nucleus ,Splicing factor ,medicine.anatomical_structure ,Microscopy, Fluorescence ,Gene Expression Regulation, Plant ,Gene expression ,RNA splicing ,Organelle ,medicine ,Nucleus ,Plant Physiological Phenomena - Abstract
The cell nucleus is a membrane-surrounded organelle that contains numerous compartments in addition to chromatin. Compartmentalization of the nucleus is now accepted as an important feature for the organization of nuclear processes and for gene expression. Recent studies on nuclear organization of splicing factors in plant cells provide insights into the compartmentalization of the plant cell nuclei and conservation of nuclear compartments between plants and metazoans.
- Published
- 2004
6. Proto-oncoprotein tls/fus is associated to the nuclear matrix and complexed with splicing factors ptb, srm160, and sr proteins
- Author
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Georg Sauermann, Josef Gotzmann, Andrea Barta, Sergiy Lopato, and Michael Meissner
- Subjects
RNA Splicing ,Biology ,Splicing factor ,SR protein ,Nuclear Matrix-Associated Proteins ,Transcription (biology) ,Proto-Oncogene Proteins ,Coactivator ,Humans ,Nuclear Matrix ,Viral matrix protein ,RNA-Binding Proteins ,Antigens, Nuclear ,Cell Biology ,Nuclear matrix ,Precipitin Tests ,Cell biology ,Microscopy, Fluorescence ,RNA splicing ,Spliceosomes ,Cancer research ,Nucleic acid ,RNA-Binding Protein FUS ,Signal Recognition Particle ,HeLa Cells ,Polypyrimidine Tract-Binding Protein ,Protein Binding - Abstract
TLS/FUS is a nucleic acid-binding protein whose N-terminal half functions as a transcriptional activator domain in fusion oncoproteins found in human leukemias and liposarcomas. Previous reports have suggested a role for TLS/FUS in transcription and splicing processes. Here we report the association of TLS/FUS with the nuclear matrix and investigate its role in splicing. Splicing of two pre-mRNAs was inhibited in a TLS/FUS-immunodepleted extract and could only be partly restored by addition of recombinant TLS/FUS or/and SR proteins, known interaction partners of TLS/FUS. The subsequent analysis of TLS/FUS immunoprecipitates revealed that, in addition to the SR proteins SC35 and SRp75, the splicing factor PTB (hnRNPI) and the splicing coactivator SRm160 are complexed with TLS/FUS, thus explaining the inability to restore splicing completely. Coimmunolocalization confirmed the nuclear matrix association and interaction of TLS/FUS with PTB, SR proteins, and SRm160. Our results suggest that the matrix protein TLS/FUS plays a role in spliceosome assembly.
- Published
- 2003
7. Periodic Conformational Changes in rRNAMonitoring the Dynamics of Translating Ribosomes
- Author
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Sebastian Patzke and Andrea Barta
- Subjects
Cell Biology ,Molecular Biology - Published
- 2000
8. Periodic Conformational Changes in rRNA
- Author
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Norbert Polacek, Andrea Barta, Knud H. Nierhaus, and Sebastian Patzke
- Subjects
Peptidyl transferase ,Chromosomal translocation ,Cell Biology ,Ribosomal RNA ,Biology ,Cleavage (embryo) ,Ribosome ,Biochemistry ,23S ribosomal RNA ,Transfer RNA ,Protein biosynthesis ,biology.protein ,Biophysics ,Molecular Biology - Abstract
In protein synthesis, a tRNA transits the ribosome via consecutive binding to the A (acceptor), P (peptidyl), and E (exit) site; these tRNA movements are catalyzed by elongation factor G (EF-G) and GTP. Site-specific Pb2+ cleavage was applied to trace tertiary alterations in tRNA and all rRNAs on pre- and posttranslocational ribosomes. The cleavage pattern of deacylated tRNA and AcPhe-tRNA changed individually upon binding to the ribosome; however, these different conformations were unaffected by translocation. On the other hand, translocation affects 23S rRNA structure. Significantly, the Pb2+ cleavage pattern near the peptidyl transferase center was different before and after translocation. This structural rearrangement emerged periodically during elongation, thus providing evidence for a dynamic and mobile role of 23S rRNA in translocation.
- Published
- 2000
9. Effects of Cadmium on Tobacco: Synthesis and Regulation of Cadmium-binding Peptides
- Author
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Andrea Barta, Karin Sommergruber, and Heribert Hirt
- Subjects
chemistry.chemical_classification ,Cadmium ,biology ,Nicotiana tabacum ,chemistry.chemical_element ,General Medicine ,General Chemistry ,Cycloheximide ,urologic and male genital diseases ,biology.organism_classification ,De novo synthesis ,chemistry.chemical_compound ,Enzyme ,chemistry ,Biochemistry ,Biosynthesis ,Cell culture ,Buthionine sulfoximine ,hormones, hormone substitutes, and hormone antagonists - Abstract
Summary Cadmium treatment of N. tabacum cv. Xanthi suspension cultured cells induced the de novo synthesis of Cd-binding peptides (Cd-BPs), which were found to consist of a mixture of (γ-glu-cys) 4 -gly and (γ-glu-cys) 5 -gly. Synthesis of Cd-BPs was inhibited by buthionine sulfoximine, a specific inhibitor of the γ-glutamyl-cysteine synthetase. Furthermore, inhibition of Cd-BP levels by cycloheximide and α-amanitin suggested that a Cd-inducible and transcriptionally regulated enzyme is responsible for the production of the Cd-BPs. In addition, the use of these inhibitors resulted in a dramatic enhancement of Cd toxicity at otherwise harmless Cd concentrations. This implies that in tobacco, chelation by de novo synthesized Cd-BPs represents the main detoxification mechanism for Cd.
- Published
- 1990
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