Extended Recognition of the Histone H3 Tail by Histone Demethylase KDM5A.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
11 02 2020
11 02 2020
Historique:
pubmed:
28
1
2020
medline:
28
7
2020
entrez:
28
1
2020
Statut:
ppublish
Résumé
Human lysine demethylase KDM5A is a chromatin-modifying enzyme associated with transcriptional regulation, because of its ability to catalyze removal of methyl groups from methylated lysine 4 of histone H3 (H3K4me3). Amplification of KDM5A is observed in many cancers, including breast cancer, prostate cancer, hepatocellular carcinoma, lung cancer, and gastric cancer. In this study, we employed alanine scanning mutagenesis to investigate substrate recognition of KDM5A and identify the H3 tail residues necessary for KDM5A-catalyzed demethylation. Our data show that the H3Q5 residue is critical for substrate recognition by KDM5A. Our data also reveal that the protein-protein interactions between KDM5A and the histone H3 tail extend beyond the amino acids proximal to the substrate mark. Specifically, demethylation activity assays show that deletion or mutation of residues at positions 14-18 on the H3 tail results in an 8-fold increase in the
Identifiants
pubmed: 31985200
doi: 10.1021/acs.biochem.9b01036
pmc: PMC7207076
mid: NIHMS1583233
doi:
Substances chimiques
Histones
0
KDM5A protein, human
EC 1.14.11.-
Retinoblastoma-Binding Protein 2
EC 1.14.11.27
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
647-651Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM114044
Pays : United States
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