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@article{708615,
author = {Papouli, Efterpi and Chen, Shuhua and Davies, Adelina and Huttner, Diana and Krejci, Lumir and Sung, Patrick and Ulrich, Helle},
article_number = {1},
keywords = {PCNA; Srs2; SUMO; repair; replication},
language = {eng},
issn = {1097-2765},
journal = {Molecular Cell},
title = {Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum},
volume = {19},
year = {2005}
}
TY - JOUR
ID - 708615
AU - Papouli, Efterpi - Chen, Shuhua - Davies, Adelina - Huttner, Diana - Krejci, Lumir - Sung, Patrick - Ulrich, Helle
PY - 2005
TI - Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.
JF - Molecular Cell
VL - 19
IS - 1
SP - 123-33
EP - 123-33
SN - 10972765
KW - PCNA
KW - Srs2
KW - SUMO
KW - repair
KW - replication
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum
L2 - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=15989970&query_hl=20&itool=pubmed_docsum
N2 - Posttranslational modification of proliferating cell nuclear antigen (PCNA), an essential processivity clamp for DNA polymerases, by ubiquitin and SUMO contributes to the coordination of DNA replication, damage tolerance, and mutagenesis. Whereas ubiquitination in response to DNA damage promotes the bypass of replication-blocking lesions, sumoylation during S phase is damage independent. As both modifiers target the same site on PCNA, an antagonistic action of SUMO on ubiquitin-dependent DNA damage tolerance has been proposed. We now present evidence that the apparent negative effect of SUMO on lesion bypass is not due to competition with ubiquitination but is rather mediated by the helicase Srs2p, which affects genome stability by suppressing unscheduled homologous recombination. We show that Srs2p physically interacts with sumoylated PCNA, which contributes to the recruitment of the helicase to replication forks. Our findings suggest a mechanism by which SUMO and ubiquitin cooperatively control the choice of pathway for the processing of DNA lesions during replication.
ER -
PAPOULI, Efterpi, Shuhua CHEN, Adelina DAVIES, Diana HUTTNER, Lumir KREJCI, Patrick SUNG a Helle ULRICH. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. \textit{Molecular Cell}. 2005, roč.~19, č.~1, s.~123-33, 10 s. ISSN~1097-2765.
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