SUPT3H-less SAGA coactivator can assemble and function without significantly perturbing RNA polymerase II transcription in mammalian cells.
Animals
DNA-Binding Proteins
/ genetics
Histone Acetyltransferases
/ metabolism
Histones
/ genetics
Humans
Mice
RNA Polymerase II
/ metabolism
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ metabolism
Trans-Activators
/ metabolism
Transcription Factors
/ metabolism
Transcription, Genetic
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
12 08 2022
12 08 2022
Historique:
accepted:
12
07
2022
revised:
05
07
2022
received:
30
05
2022
pubmed:
25
7
2022
medline:
16
8
2022
entrez:
24
7
2022
Statut:
ppublish
Résumé
Coactivator complexes regulate chromatin accessibility and transcription. SAGA (Spt-Ada-Gcn5 Acetyltransferase) is an evolutionary conserved coactivator complex. The core module scaffolds the entire SAGA complex and adopts a histone octamer-like structure, which consists of six histone-fold domain (HFD)-containing proteins forming three histone-fold (HF) pairs, to which the double HFD-containing SUPT3H adds one HF pair. Spt3, the yeast ortholog of SUPT3H, interacts genetically and biochemically with the TATA binding protein (TBP) and contributes to global RNA polymerase II (Pol II) transcription. Here we demonstrate that (i) SAGA purified from human U2OS or mouse embryonic stem cells (mESC) can assemble without SUPT3H, (ii) SUPT3H is not essential for mESC survival, but required for their growth and self-renewal, and (iii) the loss of SUPT3H from mammalian cells affects the transcription of only a specific subset of genes. Accordingly, in the absence of SUPT3H no major change in TBP accumulation at gene promoters was observed. Thus, SUPT3H is not required for the assembly of SAGA, TBP recruitment, or overall Pol II transcription, but plays a role in mESC growth and self-renewal. Our data further suggest that yeast and mammalian SAGA complexes contribute to transcription regulation by distinct mechanisms.
Identifiants
pubmed: 35871303
pii: 6649377
doi: 10.1093/nar/gkac637
pmc: PMC9371916
doi:
Substances chimiques
DNA-Binding Proteins
0
Histones
0
SPT3 protein, S cerevisiae
0
SUPT3H protein, human
0
Saccharomyces cerevisiae Proteins
0
Trans-Activators
0
Transcription Factors
0
Histone Acetyltransferases
EC 2.3.1.48
RNA Polymerase II
EC 2.7.7.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
7972-7990Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM139564
Pays : United States
Informations de copyright
© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.
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