Elucidation of the functional roles of the Q and I motifs in the human chromatin-remodeling enzyme BRG1.
ATP
ATPase
ATPase domain
BRG1
SF2 helicase family
cell cycle
cell proliferation
chromatin remodeling
nucleosome
tumor suppressor gene
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
01 03 2019
01 03 2019
Historique:
received:
03
09
2018
revised:
08
01
2019
pubmed:
17
1
2019
medline:
7
5
2019
entrez:
17
1
2019
Statut:
ppublish
Résumé
The Snf2 proteins, comprising 53 different enzymes in humans, belong to the SF2 family. Many Snf2 enzymes possess chromatin-remodeling activity, requiring a functional ATPase domain consisting of conserved motifs named Q and I-VII. These motifs form two recA-like domains, creating an ATP-binding pocket. Little is known about the function of the conserved motifs in chromatin-remodeling enzymes. Here, we characterized the function of the Q and I (Walker I) motifs in hBRG1 (SMARCA4). The motifs are in close proximity to the bound ATP, suggesting a role in nucleotide binding and/or hydrolysis. Unexpectedly, when substituting the conserved residues Gln
Identifiants
pubmed: 30647132
pii: S0021-9258(20)39260-7
doi: 10.1074/jbc.RA118.005685
pmc: PMC6398141
doi:
Substances chimiques
Nuclear Proteins
0
Nucleosomes
0
Transcription Factors
0
Adenosine Triphosphate
8L70Q75FXE
SMARCA4 protein, human
EC 3.6.1.-
DNA Helicases
EC 3.6.4.-
Banques de données
PDB
['3MWY']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3294-3310Informations de copyright
© 2019 Hoffmeister et al.
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