Methylation of histone H3 at lysine 37 by Set1 and Set2 prevents spurious DNA replication.

DNA Replication DNA, Fungal / biosynthesis Histone-Lysine N-Methyltransferase / genetics Histones / genetics Methylation Methyltransferases / genetics Saccharomyces cerevisiae / genetics Saccharomyces cerevisiae Proteins / genetics
H3K37methylation Histone modifications MCM Origin licensing Replication origins Set1 Set2

Journal

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

Informations de publication

Date de publication:
01 07 2021
Historique:
received: 13 05 2020
revised: 09 02 2021
accepted: 21 04 2021
pubmed: 13 5 2021
medline: 28 7 2021
entrez: 12 5 2021
Statut: ppublish

Résumé

DNA replication initiates at genomic locations known as origins of replication, which, in S. cerevisiae, share a common DNA consensus motif. Despite being virtually nucleosome-free, origins of replication are greatly influenced by the surrounding chromatin state. Here, we show that histone H3 lysine 37 mono-methylation (H3K37me1) is catalyzed by Set1p and Set2p and that it regulates replication origin licensing. H3K37me1 is uniformly distributed throughout most of the genome, but it is scarce at replication origins, where it increases according to the timing of their firing. We find that H3K37me1 hinders Mcm2 interaction with chromatin, maintaining low levels of MCM outside of conventional replication origins. Lack of H3K37me1 results in defective DNA replication from canonical origins while promoting replication events at inefficient and non-canonical sites. Collectively, our results indicate that H3K37me1 ensures correct execution of the DNA replication program by protecting the genome from inappropriate origin licensing and spurious DNA replication.

Identifiants

DOI: 10.1016/j.molcel.2021.04.021 PMID: 33979575 PMC: PMC7612968
pubmed: 33979575
pii: S1097-2765(21)00326-9
doi: 10.1016/j.molcel.2021.04.021
pmc: PMC7612968
mid: EMS146380
pii:
doi:

Substances chimiques

DNA, Fungal 0
Histones 0
Saccharomyces cerevisiae Proteins 0
Methyltransferases EC 2.1.1.-
Set2 protein, S cerevisiae EC 2.1.1.-
Histone-Lysine N-Methyltransferase EC 2.1.1.43
SET1 protein, S cerevisiae EC 2.1.1.43
MCM2 protein, S cerevisiae EC 3.6.4.12

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

2793-2807.e8

Subventions

Organisme : Wellcome Trust
ID : WT203144
Pays : United Kingdom
Organisme : Cancer Research UK
ID : RG72100
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210926/Z/18/Z
Pays : United Kingdom
Organisme : Cancer Research UK
ID : A18061
Pays : United Kingdom
Organisme : Cancer Research UK
ID : RG96894
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : European Research Council
ID : 309952
Pays : International
Organisme : Wellcome Trust
ID : RG94424
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C6946/A24843
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210926
Pays : United Kingdom

Informations de copyright

Copyright © 2021 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests T.K. is a co-founder and shareholder of Abcam Plc and a co-founder of Storm Therapeutics Ltd. (Cambridge, UK). T.L. is a consultant for Storm Therapeutics Ltd.

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Auteurs

Helena Santos-Rosa (H)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK. Electronic address: hsrs2@gurdon.cam.ac.uk.

Gonzalo Millán-Zambrano (G)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK; Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER), 41092 Sevilla, Spain.

Namshik Han (N)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK; Milner Therapeutics Institute, University of Cambridge, Cambridge CB2 0AW, UK.

Tommaso Leonardi (T)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK; Center for Genomic Science Istituto Italiano di Tecnologia (IIT), 20139 Milano, Italy.

Marie Klimontova (M)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.

Simona Nasiscionyte (S)

Institute of Functional Epigenetics, Helmholtz Zentrum München, 85764 Neuherberg, Germany.

Luca Pandolfini (L)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK; Istituto Italiano di Tecnologia (IIT), Center for Human Technologies (CHT), 16152 Genova, Italy.

Kostantinos Tzelepis (K)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK; Wellcome Sanger Institute, Wellcome Genome Campus, Cambridge CB10 1SA, UK.

Till Bartke (T)

Institute of Functional Epigenetics, Helmholtz Zentrum München, 85764 Neuherberg, Germany.

Tony Kouzarides (T)

The Gurdon Institute and Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK. Electronic address: t.kouzarides@gurdon.cam.ac.uk.

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Classifications MeSH

questionsmedicales.fr › Phénomènes génétiques › Réplication de l'ADN › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ADN › ADN fongique › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Protein Methyltransferases › Histone méthyltransférases › Histone-lysine N-methyltransferase › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Histone › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Métabolisme › Alkylation › Méthylation › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Methylation of histone H3 at lysine 37 by Set1...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › Methylation of histone H3 at lysine 37 by Set1...