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Structural Basis of Ubiquitin Recognition by Translesion Synthesis DNA Polymerase ι

机译：跨合成DNA聚合酶ι识别泛素的结构基础。

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Cells have evolved mutagenic bypass mechanisms that prevent stalling of the replicationnmachinery at DNA lesions. This process, translesion DNA synthesis (TLS), involves switching from high-nfidelity DNA polymerases to specialized DNA polymerases that replicate through a variety of DNA lesions.nIn eukaryotes, polymerase switching during TLS is regulated by the DNA damage-triggered monoubiqui-ntylation of PCNA. How the switch operates is unknown, but all TLS polymerases of the so-called Y-familynpossess PCNA and ubiquitin-binding domains that are important for their function. To gain insight into thenstructural mechanisms underlying the regulation of TLS by ubiquitylation, we have probed the interaction ofnubiquitin with a conserved ubiquitin-binding motif (UBM2) of Y-family polymerase Polι. Using NMRnspectroscopy, we have determined the structure of a complex of human PolιUBM2 and ubiquitin, revealing annovel ubiquitin recognition fold consisting of two R-helices separated by a central trans-proline residuenconserved in all UBMs. We show that, different from the majority of ubiquitin complexes characterized tondate, ubiquitin residue Ile44 only plays amodest role in the association of ubiquitin with PolιUBM2. Instead,nbinding of UBM2 is centered on the recognition of Leu8 in ubiquitin, which is essential for the interaction.
机译：细胞已进化出诱变旁路机制，可防止复制机器在DNA损伤处停顿。这个过程称为跨病变DNA合成（TLS），涉及从高逼真度DNA聚合酶转换成可通过各种DNA损伤复制的专门DNA聚合酶。n在真核生物中，TLS期间的聚合酶转换受DNA损伤触发的单泛素化作用调节PCNA。开关如何操作尚不清楚，但所谓的Y家族PCNA和泛素结合域的所有TLS聚合酶对其功能都很重要。为了深入了解通过泛素化作用调节TLS的潜在结构机制，我们研究了泛素与Y族聚合酶Pol1保守的泛素结合基序（UBM2）的相互作用。使用NMRn光谱法，我们已经确定了人PoluUBM2和遍在蛋白的复合物的结构，揭示了由两个R-螺旋组成的annovel遍在蛋白识别折叠，所述两个R螺旋被所有UBM中保守的中央反脯氨酸残基分隔开。我们表明，不同于大多数具有tontonate特征的泛素复合物，泛素残基Ile44仅在泛素与PolUBM2的结合中起适度的作用。相反，UBM2的结合以泛素中Leu8的识别为中心，这对于相互作用至关重要。

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