The acetyltransferase p300 is recruited in trans to multiple enhancer sites by lncSmad7.
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
21 03 2022
21 03 2022
Historique:
accepted:
25
01
2022
revised:
23
01
2022
received:
18
11
2021
pubmed:
10
2
2022
medline:
16
4
2022
entrez:
9
2
2022
Statut:
ppublish
Résumé
The histone acetyltransferase p300 (also known as KAT3B) is a general transcriptional coactivator that introduces the H3K27ac mark on enhancers triggering their activation and gene transcription. Genome-wide screenings demonstrated that a large fraction of long non-coding RNAs (lncRNAs) plays a role in cellular processes and organ development although the underlying molecular mechanisms remain largely unclear (1,2). We found 122 lncRNAs that interacts directly with p300. In depth analysis of one of these, lncSmad7, is required to maintain ESC self-renewal and it interacts to the C-terminal domain of p300. lncSmad7 also contains predicted RNA-DNA Hoogsteen forming base pairing. Combined Chromatin Isolation by RNA precipitation followed by sequencing (ChIRP-seq) together with CRISPR/Cas9 mutagenesis of the target sites demonstrate that lncSmad7 binds and recruits p300 to enhancers in trans, to trigger enhancer acetylation and transcriptional activation of its target genes. Thus, these results unveil a new mechanism by which p300 is recruited to the genome.
Identifiants
pubmed: 35137201
pii: 6523806
doi: 10.1093/nar/gkac083
pmc: PMC8934626
doi:
Substances chimiques
Chromatin
0
Histones
0
RNA, Long Noncoding
0
Acetyltransferases
EC 2.3.1.-
p300-CBP Transcription Factors
EC 2.3.1.48
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2587-2602Informations de copyright
© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.
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