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首页> 外文期刊>The FEBS journal >The N-terminal region of the bacterial DNA polymerase PolC features a pair of domains, both distantly related to domain V of the DNA polymerase III tau subunit
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The N-terminal region of the bacterial DNA polymerase PolC features a pair of domains, both distantly related to domain V of the DNA polymerase III tau subunit

机译：细菌DNA聚合酶PolC的N端区域具有一对结构域，两者都与DNA聚合酶III tau亚基的结构域V密切相关

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摘要

PolC is one of two essential replicative DNA polymerases in Bacillus subtilis and other Gram-positive bacteria. The 3D structure of PolC has recently been solved, yet it lacks the N-terminal region. For this PolC region of similar to 230 residues, both the structure and function are unknown. In the present study, using sensitive homology detection and comparative protein structure modeling, we identified, in this enigmatic region, two consecutive globular domains, PolC-NI and PolC-NII, which are followed by an apparently unstructured linker. Unexpectedly, we found that both domains are related to domain V of the tau subunit, which is part of the bacterial DNA polymerase III holoenzyme. Despite their common homology to tau, PolCNI and PolC-NII exhibit very little sequence similarity to each other. This observation argues against simple tandem duplication within PolC as the origin of the two-domain structure. Using the derived structural models, we analyzed residue conservation and the surface properties of both PolC N-terminal domains. We detected a surface patch of positive electrostatic potential in PolC-NI and a hydrophobic surface patch in PolC-NII, suggesting their possible involvement in nucleic acid and protein binding, respectively. PolC is known to interact with the tau subunit, however, the region responsible for this interaction is unknown. We propose that the PolC N-terminus is involved in mediating the PolC-tau interaction and possibly also in binding DNA.
机译：PolC是枯草芽孢杆菌和其他革兰氏阳性细菌中两种必不可少的复制性DNA聚合酶之一。 PolC的3D结构最近已得到解决，但缺少N端区域。对于类似于230个残基的PolC区域，结构和功能均未知。在本研究中，使用敏感的同源性检测和比较蛋白结构建模，我们在这个神秘区域中确定了两个连续的球状结构域PolC-NI和PolC-NII，其后是一个明显的非结构化接头。出乎意料的是，我们发现两个域都与tau亚基的域V相关，tau亚基是细菌DNA聚合酶III全酶的一部分。尽管与tau具有相同的同源性，但PolCNI和PolC-NII彼此之间几乎没有序列相似性。该观察结果反对PolC中简单的串联重复是两域结构的起源。使用衍生的结构模型，我们分析了两个PolC N末端结构域的残基保守性和表面性质。我们在PolC-NI中检测到具有正静电势的表面补丁，并在PolC-NII中检测到疏水性表面补丁，表明它们可能分别参与了核酸和蛋白质结合。已知PolC与tau亚基相互作用，但是，负责该相互作用的区域是未知的。我们建议PolC N末端参与介导PolC-tau相互作用，并可能还参与结合DNA。

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