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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Papouli E,Chen S,Davies AA,Huttner D,Krejci L,Sung P,Ulrich HDdoi
10.1016/j.molcel.2005.06.001subject
Has Abstractpub_date
2005-07-01 00:00:00pages
123-33issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(05)01376-6journal_volume
19pub_type
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