PAPOULI, Efterpi, Shuhua CHEN, Adelina DAVIES, Diana HUTTNER, Lumir KREJCI, Patrick SUNG and Helle ULRICH. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Molecular Cell. 2005, vol. 19, No 1, p. 123-33, 10 pp. ISSN 1097-2765.
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Basic information
Original name Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.
Name in Czech Komunikace mezi SUMO a ubiquitinem na PCNA je zprostředkována Srs2 proteinem
Authors PAPOULI, Efterpi (826 United Kingdom of Great Britain and Northern Ireland), Shuhua CHEN (826 United Kingdom of Great Britain and Northern Ireland), Adelina DAVIES (826 United Kingdom of Great Britain and Northern Ireland), Diana HUTTNER (826 United Kingdom of Great Britain and Northern Ireland), Lumir KREJCI (203 Czech Republic, guarantor), Patrick SUNG (840 United States of America) and Helle ULRICH (276 Germany).
Edition Molecular Cell, 2005, 1097-2765.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 14.971
Organization unit Faculty of Science
UT WoS 000230282400011
Keywords in English PCNA; Srs2; SUMO; repair; replication
Tags PCNA, repair, replication, Srs2, SUMO
Tags International impact, Reviewed
Changed by Changed by: doc. Mgr. Lumír Krejčí, Ph.D., učo 18098. Changed: 20/6/2009 06:39.
Abstract
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.
Abstract (in Czech)
Vliv post-translační modifikace PCNA na interakci s Srs2 proteinem
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