Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA.
FEBS Lett. 2012 Sep 21;586(19):3051-6. doi: 10.1016/j.febslet.2012.07.021. Epub 2012 Jul 22.
Human Rev1 is a translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap-filling. Rev1 plays an essential structural role in TLS by providing a binding platform for other TLS polymerases that insert nucleotides across DNA lesions (polη, polι, polκ) and extend the distorted primer-terminus (polς). We use NMR spectroscopy to demonstrate that the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' polη and Rev7 subunit of the 'extender' polς, thereby serving as a cassette that may accommodate several polymerases making them instantaneously available for TLS.
人 Rev1 是一种跨损伤合成（TLS）DNA 聚合酶，参与跨越 DNA 损伤部位的复制和复制后间隙填充。Rev1 通过为其他 TLS 聚合酶提供结合平台，在 TLS 中发挥着重要的结构作用，这些聚合酶可以在 DNA 损伤部位插入核苷酸（polη、polι、polκ）并延伸扭曲的引物末端（polς）。我们使用 NMR 光谱证明，Rev1 C 端结构域利用独立的相互作用界面，同时结合“插入酶”polη 的一个片段和“延伸酶”polς 的 Rev7 亚基，从而充当一个盒状结构，可以容纳多个聚合酶，使它们能够立即用于 TLS。
