Molecular Chaperone Hsp90 Regulates REV1-Mediated Mutagenesis
作者： F. Mayca Pozo , T. Oda , T. Sekimoto , Y. Murakumo , C. Masutani
DOI: 10.1128/MCB.05117-11
关键词:
摘要: REV1 is a Y-family polymerase that plays central role in mutagenic translesion DNA synthesis (TLS), contributing to tumor initiation and progression. In current model, monoubiquitinated form of the replication accessory protein, proliferating cell nuclear antigen (PCNA), serves as platform recruit damaged sites on template. Emerging evidence indicates posttranslational mechanisms regulate yeast; however, regulation higher eukaryotes poorly understood. Here we show molecular chaperone Hsp90 critical regulator human cells. specifically binds vivo vitro. Treatment with specific inhibitor reduces protein levels several types through proteasomal degradation. This associated suppression UV-induced mutagenesis. Furthermore, inhibition disrupts interaction between PCNA suppresses focus formation. These results indicate promotes folding into stable and/or functional form(s) bind PCNA. The present findings reveal novel TLS-mediated
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