Mutasome 组装因子 REV1 与泛素相互作用的结构基础。
Structural Basis for the Interaction of Mutasome Assembly Factor REV1 with Ubiquitin.
机构信息
Department of Biochemistry and Molecular Biology, Mayo Clinic, 200 First Street SW, Rochester, MN 55905, USA.
Department of Biochemistry and Molecular Biology, Mayo Clinic, 200 First Street SW, Rochester, MN 55905, USA.
出版信息
J Mol Biol. 2018 Jul 6;430(14):2042-2050. doi: 10.1016/j.jmb.2018.05.017. Epub 2018 May 18.
Abstract
REV1 is an evolutionarily conserved translesion synthesis (TLS) DNA polymerase and an assembly factor key for the recruitment of other TLS polymerases to DNA damage sites. REV1-mediated recognition of ubiquitin in the proliferative cell nuclear antigen is thought to be the trigger for TLS activation. Here we report the solution NMR structure of a 108-residue fragment of human REV1 encompassing the two putative ubiquitin-binding motifs UBM1 and UBM2 in complex with ubiquitin. While in mammals UBM1 and UBM2 are both required for optimal association of REV1 with replication factories after DNA damage, we show that only REV1 UBM2 binds ubiquitin. Structure-guided mutagenesis in Saccharomyces cerevisiae further highlights the importance of UBM2 for REV1-mediated mutagenesis and DNA damage tolerance.
摘要
REV1 是一种进化上保守的跨损伤合成（TLS）DNA 聚合酶，也是一种组装因子，对于将其他 TLS 聚合酶招募到 DNA 损伤部位至关重要。REV1 介导的对增殖细胞核抗原中泛素的识别被认为是 TLS 激活的触发因素。在这里，我们报告了人 REV1 的一个包含两个假定泛素结合基序 UBM1 和 UBM2 的 108 个残基片段与泛素的复合物的溶液 NMR 结构。虽然在哺乳动物中，UBM1 和 UBM2 都对 DNA 损伤后 REV1 与复制工厂的最佳结合是必需的，但我们表明只有 REV1 UBM2 结合泛素。酿酒酵母中的结构导向诱变进一步强调了 UBM2 对于 REV1 介导的突变和 DNA 损伤耐受的重要性。
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