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Start Over Author "Labarre-Mariotte, Sylvie" Topic saccharomyces cerevisiae
2 results on '"Labarre-Mariotte, Sylvie"'

1. Translational activators and mitoribosomal isoforms cooperate to mediate mRNA-specific translation in Schizosaccharomyces pombe mitochondria.

Author

Herbert CJ, Labarre-Mariotte S, Cornu D, Sophie C, Panozzo C, Michel T, Dujardin G, and Bonnefoy N

Subjects
Computational Biology methods, Cytochromes b genetics, Cytochromes b metabolism, DNA, Mitochondrial genetics, DNA, Mitochondrial metabolism, Electron Transport Chain Complex Proteins metabolism, Electron Transport Complex IV genetics, Electron Transport Complex IV metabolism, Gene Expression Regulation, Fungal, Mitochondria metabolism, Oxidative Phosphorylation, Protein Isoforms genetics, Protein Isoforms metabolism, RNA Stability, RNA, Messenger metabolism, RNA, Mitochondrial metabolism, Ribosomes genetics, Ribosomes metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins genetics, Saccharomyces cerevisiae Proteins metabolism, Schizosaccharomyces metabolism, Trans-Activators genetics, Trans-Activators metabolism, Electron Transport Chain Complex Proteins genetics, Mitochondria genetics, Protein Biosynthesis, RNA, Messenger genetics, RNA, Mitochondrial genetics, Saccharomyces cerevisiae genetics, Schizosaccharomyces genetics
Abstract

Mitochondrial mRNAs encode key subunits of the oxidative phosphorylation complexes that produce energy for the cell. In Saccharomyces cerevisiae, mitochondrial translation is under the control of translational activators, specific to each mRNA. In Schizosaccharomyces pombe, which more closely resembles the human system by its mitochondrial DNA structure and physiology, most translational activators appear to be either lacking, or recruited for post-translational functions. By combining bioinformatics, genetic and biochemical approaches we identified two interacting factors, Cbp7 and Cbp8, controlling Cytb production in S. pombe. We show that their absence affects cytb mRNA stability and impairs the detection of the Cytb protein. We further identified two classes of Cbp7/Cbp8 partners and showed that they modulated Cytb or Cox1 synthesis. First, two isoforms of bS1m, a protein of the small mitoribosomal subunit, that appear mutually exclusive and confer translational specificity. Second, a complex of four proteins dedicated to Cox1 synthesis, which includes an RNA helicase that interacts with the mitochondrial ribosome. Our results suggest that S. pombe contains, in addition to complexes of translational activators, a heterogeneous population of mitochondrial ribosomes that could specifically modulate translation depending on the mRNA translated, in order to optimally balance the production of different respiratory complex subunits., (© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)

Published
2021
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2. Two RNA polymerase I subunits control the binding and release of Rrn3 during transcription

Author

Beckouet, Frédéric, Labarre-Mariotte, Sylvie, Albert, Benjamin, Imazawa, Yukiko, Werner, Michel, Gadal, Olivier, Nogi, Yasuhisa, Kwapisz, Marta, BECKOUET, Frederic, Thuriaux, Pierre, Service de Biologie Intégrative et Génétique Moléculaire (SBIGeM), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Laboratoire de biologie moléculaire eucaryote (LBME), Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Service de Biologie Intégrative et Génétique Moléculaire ( SBIGeM ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de biologie moléculaire eucaryote du CNRS ( LBME ), Université Paul Sabatier - Toulouse 3 ( UPS ) -Centre National de la Recherche Scientifique ( CNRS ), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), and Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, MESH : Molecular Sequence Data, MESH : Transcription Factors, Transcription, Genetic, MESH: RNA Polymerase I, MESH: Sequence Homology, Amino Acid, [SDV]Life Sciences [q-bio], MESH : Protein Subunits, MESH : Saccharomyces cerevisiae, RNA polymerase II, MESH: Amino Acid Sequence, chemistry.chemical_compound, MESH : Mycophenolic Acid, 0302 clinical medicine, MESH: Saccharomyces cerevisiae Proteins, Sigma factor, RNA Polymerase I, RNA polymerase, Enzyme Inhibitors, ComputingMilieux_MISCELLANEOUS, Polymerase, MESH: Chromatin Immunoprecipitation, 0303 health sciences, biology, MESH : RNA Polymerase I, MESH : Amino Acid Sequence, MESH : Protein Binding, Articles, MESH: Transcription Factors, MESH : Schizosaccharomyces pombe Proteins, MESH: Protein Subunits, MESH: Saccharomyces cerevisiae, MESH : Sequence Homology, Amino Acid, MESH: Schizosaccharomyces, MESH : Dimerization, MESH: Enzyme Inhibitors, Transcription factor II D, MESH : Mutation, Dimerization, Pol1 Transcription Initiation Complex Proteins, MESH: Models, Molecular, Plasmids, Protein Binding, MESH : Pol1 Transcription Initiation Complex Proteins, Chromatin Immunoprecipitation, Saccharomyces cerevisiae Proteins, MESH: Mutation, MESH : Models, Molecular, Termination factor, Molecular Sequence Data, RNA-dependent RNA polymerase, Saccharomyces cerevisiae, MESH: Two-Hybrid System Techniques, MESH : Saccharomyces cerevisiae Proteins, 03 medical and health sciences, MESH : Chromatin Immunoprecipitation, MESH: Plasmids, Two-Hybrid System Techniques, Schizosaccharomyces, RNA polymerase I, MESH: Protein Binding, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, MESH: Pol1 Transcription Initiation Complex Proteins, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: Mycophenolic Acid, MESH : Enzyme Inhibitors, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, MESH: Transcription, Genetic, MESH : Transcription, Genetic, MESH: Schizosaccharomyces pombe Proteins, Cell Biology, Mycophenolic Acid, Molecular biology, Protein Subunits, chemistry, MESH : Schizosaccharomyces, MESH : Two-Hybrid System Techniques, MESH: Dimerization, MESH : Plasmids, Mutation, biology.protein, Schizosaccharomyces pombe Proteins, 030217 neurology & neurosurgery, Transcription Factors
Abstract

International audience; Rpa34 and Rpa49 are nonessential subunits of RNA polymerase I, conserved in species from Saccharomyces cerevisiae and Schizosaccharomyces pombe to humans. Rpa34 bound an N-terminal region of Rpa49 in a two-hybrid assay and was lost from RNA polymerase in an rpa49 mutant lacking this Rpa34-binding domain, whereas rpa34Delta weakened the binding of Rpa49 to RNA polymerase. rpa34Delta mutants were caffeine sensitive, and the rpa34Delta mutation was lethal in a top1Delta mutant and in rpa14Delta, rpa135(L656P), and rpa135(D395N) RNA polymerase mutants. These defects were shared by rpa49Delta mutants, were suppressed by the overexpression of Rpa49, and thus, were presumably mediated by Rpa49 itself. rpa49 mutants lacking the Rpa34-binding domain behaved essentially like rpa34Delta mutants, but strains carrying rpa49Delta and rpa49-338::HIS3 (encoding a form of Rpa49 lacking the conserved C terminus) had reduced polymerase occupancy at 30 degrees C, failed to grow at 25 degrees C, and were sensitive to 6-azauracil and mycophenolate. Mycophenolate almost fully dissociated the mutant polymerase from its ribosomal DNA (rDNA) template. The rpa49Delta and rpa49-338::HIS3 mutations had a dual effect on the transcription initiation factor Rrn3 (TIF-IA). They partially impaired its recruitment to the rDNA promoter, an effect that was bypassed by an N-terminal deletion of the Rpa43 subunit encoded by rpa43-35,326, and they strongly reduced the release of the Rrn3 initiation factor during elongation. These data suggest a dual role of the Rpa49-Rpa34 dimer during the recruitment of Rrn3 and its subsequent dissociation from the elongating polymerase.

Published
2008
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