@article{oai:repo.qst.go.jp:00046014,
 author = {Schmutz, Valerie and Janel-Bintz, Regine and Wagner, Jerome and Biard, Denis and Shiomi, Naoko and P., Fuchs Robert and M., Cordonnier Agnes and 塩見 尚子},
 issue = {19},
 journal = {Nucleic Acids Research},
 month = {Jun},
 note = {In eukaryotic cells, the Rad6/Rad18-dependent monoubiquitination of the proliferating cell nuclear antigen (PCNA) plays an essential role in the switching between replicatin and translesion DNA synthesis (TLS).The DNA polymerase PolHbinds to PCNA via a consensus C-terminal PCNA-interacting protein ( PIP) motif. It also specifically interacts with monoubiquitinated PCNA thanks to a recently identified ubiquitin-binding domain (UBZ).To investigate whether the TLS activity of PolHis always coupled to PCNA monoubiquitination, we monitor the ability of cell-free extracts to perform DNA synthesis across different types of lesions. We observe that a cis-syncyclobutane thymine dimer (TT-CPD),but not a N-2-2acetylaminouorene-guanine (G-AAF) adduct, is efficiently bypassed in extracts from Rad18-deficient cells, thus demonstrating the existence of a PolH -dependent and Rad18-independent TLS pathway .In addition ,by complementing PolH -deficient cells with PIP and UBZ mutants, we show that each of these domains contributes to PolH activity. The finding that the bypass of a CPD lesion in vitro does not require Ub-PCNA but nevertheless depends on the UBZ domain of PolH, reveals that this domain may play a novel role in the TLS process that is not related to the monoubiquitination status of  PCNA.},
 pages = {6456--6465},
 title = {Role of the ubiquitin-binding domain of PolH in RaD 18-independent translesion DNA synthesis in human cell extracts},
 volume = {38},
 year = {2010}
}