Linker DNA and histone contributions in nucleosome binding by p53.
chromatin
histone
nucleosome
p53
pioneer transcription factor
Journal
Journal of biochemistry
ISSN: 1756-2651
Titre abrégé: J Biochem
Pays: England
ID NLM: 0376600
Informations de publication
Date de publication:
26 Dec 2020
26 Dec 2020
Historique:
received:
01
06
2020
accepted:
13
07
2020
pubmed:
24
7
2020
medline:
1
6
2021
entrez:
24
7
2020
Statut:
ppublish
Résumé
The tumour suppressor protein p53 regulates various genes involved in cell-cycle arrest, apoptosis and DNA repair in response to cellular stress, and apparently functions as a pioneer transcription factor. The pioneer transcription factors can bind nucleosomal DNA, where many transcription factors are largely restricted. However, the mechanisms by which p53 recognizes the nucleosomal DNA are poorly understood. In the present study, we found that p53 requires linker DNAs for the efficient formation of p53-nucleosome complexes. p53 forms an additional specific complex with the nucleosome, when the p53 binding sequence is located around the entry/exit region of the nucleosomal DNA. We also showed that p53 directly binds to the histone H3-H4 complex via its N-terminal 1-93 amino acid region. These results shed light on the mechanism of nucleosome recognition by p53.
Identifiants
pubmed: 32702132
pii: 5875610
doi: 10.1093/jb/mvaa081
pmc: PMC7763433
doi:
Substances chimiques
Histones
0
Nucleosomes
0
TP53 protein, human
0
Tumor Suppressor Protein p53
0
DNA
9007-49-2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
669-675Informations de copyright
© The Author(s) 2020. Published by Oxford University Press on behalf of the Japanese Biochemical Society.
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