Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1.
DNA
/ chemistry
DNA Damage
Fluorescence Polarization
HeLa Cells
Humans
Magnesium
/ metabolism
Microscopy, Atomic Force
Nucleic Acid Conformation
Nucleosomes
/ genetics
Poly (ADP-Ribose) Polymerase-1
/ chemistry
Poly Adenosine Diphosphate Ribose
/ metabolism
Protein Binding
Protein Multimerization
Protein Processing, Post-Translational
Y-Box-Binding Protein 1
/ chemistry
Y-box-binding protein 1
poly(ADP-ribose) polymerase 1
protein poly(ADP-ribosyl)ation
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
16 09 2020
16 09 2020
Historique:
received:
10
07
2020
revised:
07
09
2020
accepted:
10
09
2020
entrez:
19
9
2020
pubmed:
20
9
2020
medline:
14
9
2021
Statut:
epublish
Résumé
Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg
Identifiants
pubmed: 32947956
pii: biom10091325
doi: 10.3390/biom10091325
pmc: PMC7565162
pii:
doi:
Substances chimiques
Nucleosomes
0
Y-Box-Binding Protein 1
0
Poly Adenosine Diphosphate Ribose
26656-46-2
DNA
9007-49-2
PARP1 protein, human
EC 2.4.2.30
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Magnesium
I38ZP9992A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Science Foundation
ID : 19-14-00107
Pays : International
Organisme : Russian Foundation for Basic Research
ID : 20-34-70028
Pays : International
Organisme : UEVE Université Paris-Saclay
ID : CIR 2017
Pays : International
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