A Role for the Mre11-Rad50-Xrs2 Complex in Gene Expression and Chromosome Organization.

Chromosomes, Fungal / genetics DNA-Binding Proteins / genetics Endodeoxyribonucleases / genetics Exodeoxyribonucleases / genetics Gene Expression Regulation, Fungal Multiprotein Complexes / metabolism Saccharomyces cerevisiae / genetics Saccharomyces cerevisiae Proteins / genetics
MRX/N Mediator SMC complexes chromosomal interaction domains chromosome folding chromosome organization coding and non-coding transcription control nuclear pore

Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
07 01 2021
Historique:
received: 28 04 2020
revised: 03 11 2020
accepted: 05 11 2020
pubmed: 6 12 2020
medline: 28 1 2021
entrez: 5 12 2020
Statut: ppublish

Résumé

Mre11-Rad50-Xrs2 (MRX) is a highly conserved complex with key roles in various aspects of DNA repair. Here, we report a new function for MRX in limiting transcription in budding yeast. We show that MRX interacts physically and colocalizes on chromatin with the transcriptional co-regulator Mediator. MRX restricts transcription of coding and noncoding DNA by a mechanism that does not require the nuclease activity of Mre11. MRX is required to tether transcriptionally active loci to the nuclear pore complex (NPC), and it also promotes large-scale gene-NPC interactions. Moreover, MRX-mediated chromatin anchoring to the NPC contributes to chromosome folding and helps to control gene expression. Together, these findings indicate that MRX has a role in transcription and chromosome organization that is distinct from its known function in DNA repair.

Identifiants

DOI: 10.1016/j.molcel.2020.11.010 PMID: 33278361 PMC: PMC8112817
pubmed: 33278361
pii: S1097-2765(20)30788-7
doi: 10.1016/j.molcel.2020.11.010
pmc: PMC8112817
mid: NIHMS1700051
pii:
doi:

Substances chimiques

DNA-Binding Proteins 0
Multiprotein Complexes 0
RAD50 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0
XRS2 protein, S cerevisiae 0
Endodeoxyribonucleases EC 3.1.-
Exodeoxyribonucleases EC 3.1.-
MRE11 protein, S cerevisiae EC 3.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

183-197.e6

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM112131
Pays : United States

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Interests The authors declare no competing interests.

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Auteurs

Romain Forey (R)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Equipe Labéllisée Ligue contre le Cancer, 34396 Montpellier, France.

Antoine Barthe (A)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Equipe Labéllisée Ligue contre le Cancer, 34396 Montpellier, France.

Mireille Tittel-Elmer (M)

Departments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, T2N 1N4, Canada.

Maxime Wery (M)

Institut Curie, PSL Research University, CNRS UMR 3244, ncRNA, Epigenetic and Genome Fluidity, Université Pierre et Marie Curie, 26 rue d'Ulm, 75248 Paris, France.

Marie-Bénédicte Barrault (MB)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Cécile Ducrot (C)

Institute of Molecular and Cellular Radiobiology, Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA)/Direction de la Recherche Fondamentale (DRF), 92260 Fontenay-aux-Roses Cedex, France.

Andrew Seeber (A)

Center for Advanced Imaging, Harvard University, Cambridge, MA 02138, USA; University of Basel and Friedrich Miescher Institute for Biomedical Research, Faculty of Natural Sciences, Klingelbergstrasse 50, 4056 Basel, Switzerland.

Nils Krietenstein (N)

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.

Ugo Szachnowski (U)

Institut Curie, PSL Research University, CNRS UMR 3244, ncRNA, Epigenetic and Genome Fluidity, Université Pierre et Marie Curie, 26 rue d'Ulm, 75248 Paris, France.

Magdalena Skrzypczak (M)

Laboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Zwirki i Wigury 93, 02-089 Warsaw, Poland.

Krzysztof Ginalski (K)

Laboratory of Bioinformatics and Systems Biology, Centre of New Technologies, University of Warsaw, Zwirki i Wigury 93, 02-089 Warsaw, Poland.

Maga Rowicka (M)

Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX 77555, USA.

Jennifer A Cobb (JA)

Departments of Biochemistry and Molecular Biology and Oncology, Robson DNA Science Centre, Charbonneau Cancer Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, T2N 1N4, Canada.

Oliver J Rando (OJ)

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.

Julie Soutourina (J)

Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France.

Michel Werner (M)

Institut Jacques Monod, CNRS UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France.

Karine Dubrana (K)

Institute of Molecular and Cellular Radiobiology, Commissariat à l'Énergie Atomique et aux Énergies Alternatives (CEA)/Direction de la Recherche Fondamentale (DRF), 92260 Fontenay-aux-Roses Cedex, France.

Susan M Gasser (SM)

University of Basel and Friedrich Miescher Institute for Biomedical Research, Faculty of Natural Sciences, Klingelbergstrasse 50, 4056 Basel, Switzerland.

Antonin Morillon (A)

Institut Curie, PSL Research University, CNRS UMR 3244, ncRNA, Epigenetic and Genome Fluidity, Université Pierre et Marie Curie, 26 rue d'Ulm, 75248 Paris, France.

Philippe Pasero (P)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Equipe Labéllisée Ligue contre le Cancer, 34396 Montpellier, France.

Armelle Lengronne (A)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Equipe Labéllisée Ligue contre le Cancer, 34396 Montpellier, France. Electronic address: armelle.lengronne@igh.cnrs.fr.

Jérôme Poli (J)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Equipe Labéllisée Ligue contre le Cancer, 34396 Montpellier, France; University of Basel and Friedrich Miescher Institute for Biomedical Research, Faculty of Natural Sciences, Klingelbergstrasse 50, 4056 Basel, Switzerland. Electronic address: jerome.poli@igh.cnrs.fr.

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Classifications MeSH

questionsmedicales.fr › Phénomènes génétiques › Structures génétiques › Chromosomes › Chromosomes de champignon › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de liaison à l'ADN › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Esterases › Endonucleases › Endodeoxyribonucleases › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Esterases › Exonucleases › Exodeoxyribonucleases › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes fongiques › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Structures macromoléculaires › Complexes multiprotéiques › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › A Role for the Mre11-Rad50-Xrs2 Complex in...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › A Role for the Mre11-Rad50-Xrs2 Complex in...