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2. The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones

Author

Maurizy, Chloe, Quinternet, Marc, Abel, Yoann, Verheggen, Celine, Santo, Paulo E., Bourguet, Maxime, Paiva, Ana C. F., Bragantini, Benoit, Chagot, Marie-Eve, Robert, Marie-Cecile, Abeza, Claire, Fabre, Philippe, Fort, Philippe, Vandermoere, Franck, Sousa, Pedro M. F., Rain, Jean-Christophe, Charpentier, Bruno, Cianferani, Sarah, Bandeiras, Tiago M., Pradet-Balade, Berengere, Manival, Xavier, Bertrand, Edouard, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Ingénierie, Biologie et Santé en Lorraine (IBSLor), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Laboratoire de Spectrométrie de Masse BioOrganique (IPHC-DSA), Instituto de Biologia Experimental e Tecnológica (IBET), Centre de recherches de biochimie macromoléculaire (CRBM), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-IFR122-Centre National de la Recherche Scientifique (CNRS), Hybrigenics [Paris], Hybrigenics, Service de néphrologie, Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Bicêtre-Institut National de la Santé et de la Recherche Médicale (INSERM), Instituto de Tecnologia Química e Biológica António Xavier (ITQB), Universidade Nova de Lisboa (NOVA), Equipe labellisée Ligue contre le Cancer, Université de Lorraine (UL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universidade de Lisboa (ULISBOA), Laboratoire de Spectrométrie de Masse BioOrganique [Strasbourg] (LSMBO), Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut Pluridisciplinaire Hubert Curien (IPHC), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM), Laboratoire de Spectrométrie de Masse BioOrganique, Département des Sciences Analytiques, Institut Pluridisciplinaire Hubert Curien, Strasbourg, France (LSMBO-DSA-IPHC), Centre National de la Recherche Scientifique (CNRS), Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), bertrand, edouard, Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Universidade de Lisboa = University of Lisbon (ULISBOA), Centre de recherche en Biologie cellulaire de Montpellier (CRBM), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Male, AAA proteins, [SDV]Life Sciences [q-bio], General Physics and Astronomy, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Chaperone, [SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics, Phylogenetics and taxonomy, Protein Structure, Secondary, Testis, lcsh:Science, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), ComputingMilieux_MISCELLANEOUS, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV] Life Sciences [q-bio], [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Antigens, Surface, Protein Binding, Signal Transduction, Cell biology, RUVBL2, Science, [SDV.CAN]Life Sciences [q-bio]/Cancer, Hsp90, Chaperone (protein), [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Plasma protein binding, Article, General Biochemistry, Genetics and Molecular Biology, Cell Line, GTP-Binding Proteins, Genetics, Humans, GTP-binding protein regulators, HSP90 Heat-Shock Proteins, Protein folding, IP LUMIER, Adaptor Proteins, Signal Transducing, DNA Helicases, Membrane Proteins, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, General Chemistry, liprin-α2, NMR, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, HEK293 Cells, Membrane protein, ATPases Associated with Diverse Cellular Activities, lcsh:Q, Apoptosis Regulatory Proteins, Carrier Proteins, R2SP, HeLa Cells, Molecular Chaperones
Abstract

R2TP is an HSP90 co-chaperone that assembles important macro-molecular machineries. It is composed of an RPAP3-PIH1D1 heterodimer, which binds the two essential AAA+ATPases RUVBL1/RUVBL2. Here, we resolve the structure of the conserved C-terminal domain of RPAP3, and we show that it directly binds RUVBL1/RUVBL2 hexamers. The human genome encodes two other proteins bearing RPAP3-C-terminal-like domains and three containing PIH-like domains. Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-α2 expression and for the assembly of liprin-α2 complexes, indicating that R2SP functions in quaternary protein folding. Effects are stronger at 32 °C, suggesting that R2SP could help compensating the lower temperate of testis., R2TP is an HSP90 co-chaperone composed of an RPAP3-PIH1D1 heterodimer, which binds two essential AAA+ ATPases RUVBL1/RUVBL2. Here authors use a structural approach to study RPAP3 and find an RPAP3-like protein (SPAG1) which also forms a co-chaperone complex with PIH1D2 and RUVBL1/2 enriched in testis.

Published
2018

3. RiboSys, a high-resolution, quantitative approach to measure the in vivo kinetics of pre-mRNA splicing and 3'-end processing in Saccharomyces cerevisiae

Author

Alexander, Ross D., Barrass, J. David, Dichtl, Beatriz, Kos, Martin, Obtulowicz, Tomasz, Robert, Marie-Cecile, Koper, Michal, Karkusiewicz, Iwona, Mariconti, Luisa, Tollervey, David, Dichtl, Bernhard, Kufel, Joanna, Bertrand, Edouard, Beggs, Jean D., Alexander, Ross D., Barrass, J. David, Dichtl, Beatriz, Kos, Martin, Obtulowicz, Tomasz, Robert, Marie-Cecile, Koper, Michal, Karkusiewicz, Iwona, Mariconti, Luisa, Tollervey, David, Dichtl, Bernhard, Kufel, Joanna, Bertrand, Edouard, and Beggs, Jean D.

Abstract

We describe methods for obtaining a quantitative description of RNA processing at high resolution in budding yeast. As a model gene expression system, we constructed tetON (for induction studies) and tetOFF (for repression, derepression, and RNA degradation studies) yeast strains with a series of reporter genes integrated in the genome under the control of a tetO7 promoter. Reverse transcription and quantitative real-time-PCR (RT-qPCR) methods were adapted to allow the determination of mRNA abundance as the average number of copies per cell in a population. Fluorescence in situ hybridization (FISH) measurements of transcript numbers in individual cells validated the RT-qPCR approach for the average copy-number determination despite the broad distribution of transcript levels within a population of cells. In addition, RT-qPCR was used to distinguish the products of the different steps in splicing of the reporter transcripts, and methods were developed to map and quantify 3′-end cleavage and polyadenylation. This system permits pre-mRNA production, splicing, 3′-end maturation and degradation to be quantitatively monitored with unprecedented kinetic detail, suitable for mathematical modeling. Using this approach, we demonstrate that reporter transcripts are spliced prior to their 3′-end cleavage and polyadenylation, that is, cotranscriptionally.

Published
2010

4. RiboSys, a high-resolution, quantitative approach to measure the in vivo kinetics of pre-mRNA splicing and 3′-end processing in Saccharomyces cerevisiae

Author

Alexander, Ross D., primary, Barrass, J. David, additional, Dichtl, Beatriz, additional, Kos, Martin, additional, Obtulowicz, Tomasz, additional, Robert, Marie-Cecile, additional, Koper, Michal, additional, Karkusiewicz, Iwona, additional, Mariconti, Luisa, additional, Tollervey, David, additional, Dichtl, Bernhard, additional, Kufel, Joanna, additional, Bertrand, Edouard, additional, and Beggs, Jean D., additional

Published
2010
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