期刊
CELL REPORTS
卷 13, 期 10, 页码 2072-2080出版社
CELL PRESS
DOI: 10.1016/j.celrep.2015.11.014
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资金
- JSPS KAKENHI [24310040, 26550024, 26740017, 26860310, 25241011]
- MEXT KAKENHI [22131008]
- Hori Sciences and Arts Foundation
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [25241011, 26740017, 26860310, 15K14953, 22131001, 26550024] Funding Source: KAKEN
Mono-ubiquitinated PCNA activates error-prone DNA polymerases; therefore, strict regulation of PCNA mono-ubiquitination is crucial in avoiding undesired mutagenesis. In this study, we used an in vitro assay system to identify USP7 as a deubiquitinating enzyme of mono-ubiquitinated PCNA. Suppression of USP1, a previously identified PCNA deubiquitinase, or USP7 increased UV- and H2O2-induced PCNA mono-ubiquitination in a distinct and additive manner, suggesting that USP1 and USP7 make different contributions to PCNA deubiquitination in human cells. Cell-cycle-synchronization analyses revealed that USP7 suppression increased H2O2-induced PCNA ubiquitination throughout interphase, whereas USP1 suppression specifically increased ubiquitination in S-phase cells. UV-induced mutagenesis was elevated in USP1-suppressed cells, whereas H2O2-induced mutagenesis was elevated in USP7-suppressed cells. These results suggest that USP1 suppresses UV-induced mutations produced in a manner involving DNA replication, whereas USP7 suppresses H2O2-induced mutagenesis involving cell-cycle-independent processes such as DNA repair.
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