Mec1 Is Activated at the Onset of Normal S Phase by Low-dNTP Pools Impeding DNA Replication.

Cell Cycle Proteins / genetics Checkpoint Kinase 2 / genetics DNA Replication / physiology Deoxyribonucleotides / genetics Gene Expression Regulation, Fungal Intracellular Signaling Peptides and Proteins / genetics Mitosis Protein Serine-Threonine Kinases / genetics Replication Origin S Phase / physiology Saccharomyces cerevisiae / cytology Saccharomyces cerevisiae Proteins / genetics
ATR DNA replication Mec1 S phase checkpoint budding yeast cell cycle dNTP synthesis fork collapse mitotic catastrophe replication timing

Journal

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

Informations de publication

Date de publication:
07 05 2020
Historique:
received: 27 08 2019
revised: 09 01 2020
accepted: 24 02 2020
pubmed: 15 3 2020
medline: 29 8 2020
entrez: 15 3 2020
Statut: ppublish

Résumé

The Mec1 and Rad53 kinases play a central role during acute replication stress in budding yeast. They are also essential for viability in normal growth conditions, but the signal that activates the Mec1-Rad53 pathway in the absence of exogenous insults is currently unknown. Here, we show that this pathway is active at the onset of normal S phase because deoxyribonucleotide triphosphate (dNTP) levels present in G

Identifiants

DOI: 10.1016/j.molcel.2020.02.021 PMID: 32169162
pubmed: 32169162
pii: S1097-2765(20)30114-3
doi: 10.1016/j.molcel.2020.02.021
pii:
doi:

Substances chimiques

Cell Cycle Proteins 0
Deoxyribonucleotides 0
Intracellular Signaling Peptides and Proteins 0
SML1 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0
Checkpoint Kinase 2 EC 2.7.1.11
MEC1 protein, S cerevisiae EC 2.7.11.1
Protein Serine-Threonine Kinases EC 2.7.11.1
RAD53 protein, S cerevisiae EC 2.7.12.1

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

396-410.e4

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Interests The authors declare no competing interests.

Auteurs

Romain Forey (R)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France.

Ana Poveda (A)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France; Instituto de Investigación en Salud Pública y Zoonosis, Facultad de Ciencias Químicas, Universidad Central del Ecuador, Quito, Ecuador.

Sushma Sharma (S)

Department of Medical Biochemistry and Biophysics and Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå, Sweden.

Antoine Barthe (A)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France.

Ismael Padioleau (I)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France.

Claire Renard (C)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France.

Robin Lambert (R)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, 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.

Armelle Lengronne (A)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France.

Andrei Chabes (A)

Department of Medical Biochemistry and Biophysics and Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå, Sweden.

Benjamin Pardo (B)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France. Electronic address: benjamin.pardo@igh.cnrs.fr.

Philippe Pasero (P)

Institut de Génétique Humaine, CNRS, Université de Montpellier, Montpellier, France. Electronic address: philippe.pasero@igh.cnrs.fr.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cycle cellulaire › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Checkpoint kinase 2 › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Phénomènes génétiques › Réplication de l'ADN › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Désoxyribonucléotides › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes fongiques › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Phénomènes génétiques › Division du noyau cellulaire › Mitose › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Phénomènes génétiques › Structures génétiques › Génome › Composants de génome › Réplicon › Origine de réplication › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Phénomènes génétiques › Réplication de l'ADN › Phase S › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Mec1 Is Activated at the Onset of Normal S...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › Mec1 Is Activated at the Onset of Normal S...