The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance

Claudia M. Nicolae, Erin R. Aho, Alexander H.S. Vlahos, Katherine N. Choe, Subhajyoti De, Georgios Karras, George Lucian Moldovan

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

All cells rely on genomic stability mechanisms to protect against DNA alterations. PCNA is a master regulator of DNA replication and S-phase-coupled repair. PCNA post-translational modifications by ubiquitination and SUMOylation dictate how cells stabilize and re-start replication forks stalled at sites of damaged DNA.PCNAmono-ubiquitination recruits low fidelity DNA polymerases to promote error-prone replication across DNA lesions. Here, we identify the mono-ADP-ribosyltransferase PARP10/ARTD10 as a novelPCNAbinding partner. PARP10 knockdown results in genomic instability and DNA damage hypersensitivity. Importantly, we show that PARP10 binding toPCNAis required for translesionDNAsynthesis. Our work identifies a novel PCNA-linked mechanism for genome protection, centered on post-translational modification by mono-ADP-ribosylation.

Original languageEnglish (US)
Pages (from-to)13627-13637
Number of pages11
JournalJournal of Biological Chemistry
Volume289
Issue number19
DOIs
StatePublished - Jan 1 2014

Fingerprint

ADP Ribose Transferases
Damage tolerance
Proliferating Cell Nuclear Antigen
DNA Damage
Genomic Instability
Ubiquitination
Post Translational Protein Processing
DNA Replication
DNA
Sumoylation
DNA-Directed DNA Polymerase
S Phase
Adenosine Diphosphate
Hypersensitivity
Genome
Repair
Genes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance. / Nicolae, Claudia M.; Aho, Erin R.; Vlahos, Alexander H.S.; Choe, Katherine N.; De, Subhajyoti; Karras, Georgios; Moldovan, George Lucian.

In: Journal of Biological Chemistry, Vol. 289, No. 19, 01.01.2014, p. 13627-13637.

Research output: Contribution to journalArticle

Nicolae, Claudia M. ; Aho, Erin R. ; Vlahos, Alexander H.S. ; Choe, Katherine N. ; De, Subhajyoti ; Karras, Georgios ; Moldovan, George Lucian. / The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance. In: Journal of Biological Chemistry. 2014 ; Vol. 289, No. 19. pp. 13627-13637.
@article{2a9d17d0a40048d485ca9832a1f07a3f,
title = "The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance",
abstract = "All cells rely on genomic stability mechanisms to protect against DNA alterations. PCNA is a master regulator of DNA replication and S-phase-coupled repair. PCNA post-translational modifications by ubiquitination and SUMOylation dictate how cells stabilize and re-start replication forks stalled at sites of damaged DNA.PCNAmono-ubiquitination recruits low fidelity DNA polymerases to promote error-prone replication across DNA lesions. Here, we identify the mono-ADP-ribosyltransferase PARP10/ARTD10 as a novelPCNAbinding partner. PARP10 knockdown results in genomic instability and DNA damage hypersensitivity. Importantly, we show that PARP10 binding toPCNAis required for translesionDNAsynthesis. Our work identifies a novel PCNA-linked mechanism for genome protection, centered on post-translational modification by mono-ADP-ribosylation.",
author = "Nicolae, {Claudia M.} and Aho, {Erin R.} and Vlahos, {Alexander H.S.} and Choe, {Katherine N.} and Subhajyoti De and Georgios Karras and Moldovan, {George Lucian}",
year = "2014",
month = "1",
day = "1",
doi = "10.1074/jbc.M114.556340",
language = "English (US)",
volume = "289",
pages = "13627--13637",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

TY - JOUR

T1 - The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance

AU - Nicolae, Claudia M.

AU - Aho, Erin R.

AU - Vlahos, Alexander H.S.

AU - Choe, Katherine N.

AU - De, Subhajyoti

AU - Karras, Georgios

AU - Moldovan, George Lucian

PY - 2014/1/1

Y1 - 2014/1/1

N2 - All cells rely on genomic stability mechanisms to protect against DNA alterations. PCNA is a master regulator of DNA replication and S-phase-coupled repair. PCNA post-translational modifications by ubiquitination and SUMOylation dictate how cells stabilize and re-start replication forks stalled at sites of damaged DNA.PCNAmono-ubiquitination recruits low fidelity DNA polymerases to promote error-prone replication across DNA lesions. Here, we identify the mono-ADP-ribosyltransferase PARP10/ARTD10 as a novelPCNAbinding partner. PARP10 knockdown results in genomic instability and DNA damage hypersensitivity. Importantly, we show that PARP10 binding toPCNAis required for translesionDNAsynthesis. Our work identifies a novel PCNA-linked mechanism for genome protection, centered on post-translational modification by mono-ADP-ribosylation.

AB - All cells rely on genomic stability mechanisms to protect against DNA alterations. PCNA is a master regulator of DNA replication and S-phase-coupled repair. PCNA post-translational modifications by ubiquitination and SUMOylation dictate how cells stabilize and re-start replication forks stalled at sites of damaged DNA.PCNAmono-ubiquitination recruits low fidelity DNA polymerases to promote error-prone replication across DNA lesions. Here, we identify the mono-ADP-ribosyltransferase PARP10/ARTD10 as a novelPCNAbinding partner. PARP10 knockdown results in genomic instability and DNA damage hypersensitivity. Importantly, we show that PARP10 binding toPCNAis required for translesionDNAsynthesis. Our work identifies a novel PCNA-linked mechanism for genome protection, centered on post-translational modification by mono-ADP-ribosylation.

UR - http://www.scopus.com/inward/record.url?scp=84900458533&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84900458533&partnerID=8YFLogxK

U2 - 10.1074/jbc.M114.556340

DO - 10.1074/jbc.M114.556340

M3 - Article

C2 - 24695737

AN - SCOPUS:84900458533

VL - 289

SP - 13627

EP - 13637

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -