Mediator recruits the cohesin loader Scc2 to RNA Pol II-transcribed genes and promotes sister chromatid cohesion.
Med14
Mediator
Saccharomyces cerevisiae
Scc2-Scc4
chromatin adapters
cohesin
cohesin loader
sister chromatid cohesion
Journal
Current biology : CB
ISSN: 1879-0445
Titre abrégé: Curr Biol
Pays: England
ID NLM: 9107782
Informations de publication
Date de publication:
11 07 2022
11 07 2022
Historique:
received:
04
01
2021
revised:
07
04
2022
accepted:
09
05
2022
pubmed:
3
6
2022
medline:
15
7
2022
entrez:
2
6
2022
Statut:
ppublish
Résumé
The ring-like cohesin complex plays an essential role in chromosome segregation, organization, and double-strand break repair through its ability to bring two DNA double helices together. Scc2 (NIPBL in humans) together with Scc4 functions as the loader of cohesin onto chromosomes. Chromatin adapters such as the RSC complex facilitate the localization of the Scc2-Scc4 cohesin loader. Here, we identify a broad range of Scc2-chromatin protein interactions that are evolutionarily conserved and reveal a role for one complex, Mediator, in the recruitment of the cohesin loader. We identified budding yeast Med14, a subunit of the Mediator complex, as a high copy suppressor of poor growth in Scc2 mutant strains. Physical and genetic interactions between Scc2 and Mediator are functionally substantiated in direct recruitment and cohesion assays. Depletion of Med14 results in defective sister chromatid cohesion and the decreased binding of Scc2 at RNA Pol II-transcribed genes. Previous work has suggested that Mediator, Nipbl, and cohesin connect enhancers and promoters of active mammalian genes. Our studies suggest an evolutionarily conserved fundamental role for Mediator in the direct recruitment of Scc2 to RNA Pol II-transcribed genes.
Identifiants
pubmed: 35654035
pii: S0960-9822(22)00778-3
doi: 10.1016/j.cub.2022.05.019
pmc: PMC9286023
pii:
doi:
Substances chimiques
Cell Cycle Proteins
0
Chromatin
0
Chromosomal Proteins, Non-Histone
0
NIPBL protein, human
0
SCC2 protein, S cerevisiae
0
SCC4 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
RNA Polymerase II
EC 2.7.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2884-2896.e6Subventions
Organisme : Wellcome Trust
ID : FC001198
Pays : United Kingdom
Organisme : Cancer Research UK
Pays : United Kingdom
Organisme : Medical Research Council
Pays : United Kingdom
Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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