DNA Polymerase ι Interacts with Both the TRAF-like and UBL1-2 Domains of USP7.
Binding Sites
Catalytic Domain
Cell Line
DNA-Directed DNA Polymerase
/ chemistry
Humans
Kinetics
Models, Molecular
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs
Recombinant Proteins
Structure-Activity Relationship
Substrate Specificity
Ubiquitin-Specific Peptidase 7
/ chemistry
Ubiquitination
DNA Polymerase iota
DNA polymerase iota
Deubiquitination
Herpesvirus-associated ubiquitin-specific protease
Ubiquitin-like domain
Ubiquitin-specific protease 7
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
22 01 2021
22 01 2021
Historique:
received:
10
09
2020
revised:
20
11
2020
accepted:
30
11
2020
pubmed:
7
12
2020
medline:
27
4
2021
entrez:
6
12
2020
Statut:
ppublish
Résumé
Reversible protein ubiquitination is an essential signaling mechanism within eukaryotes. Deubiquitinating enzymes are critical to this process, as they mediate removal of ubiquitin from substrate proteins. Ubiquitin-specific protease 7 (USP7) is a prominent deubiquitinating enzyme, with an extensive network of interacting partners and established roles in cell cycle activation, immune responses and DNA replication. Characterized USP7 substrates primarily interact with one of two major binding sites outside the catalytic domain. These are located on the USP7 N-terminal TRAF-like (TRAF) domain and the first and second UBL domains (UBL1-2) within the C-terminal tail. Here, we report that DNA polymerase iota (Pol ι) is a novel USP7 substrate that interacts with both TRAF and UBL1-2. Through the use of biophysical approaches and mutational analysis, we characterize both interfaces and demonstrate that bipartite binding to both USP7 domains is required for efficient Pol ι deubiquitination. Together, these data establish a new bipartite mode of USP7 substrate binding.
Identifiants
pubmed: 33279577
pii: S0022-2836(20)30657-4
doi: 10.1016/j.jmb.2020.166733
pmc: PMC7873624
mid: NIHMS1660875
pii:
doi:
Substances chimiques
Recombinant Proteins
0
DNA-Directed DNA Polymerase
EC 2.7.7.7
Ubiquitin-Specific Peptidase 7
EC 3.4.19.12
DNA Polymerase iota
EC 2.7.7.7
POLI protein, human
EC 2.7.7.7
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, N.I.H., Intramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
166733Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM111135
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM123249
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM128864
Pays : United States
Informations de copyright
Published by Elsevier Ltd.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare they have no conflict of interest.
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