Rappas Mathieu, Bose Daniel, Zhang Xiaodong
Centre for Structural Biology, Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
Curr Opin Struct Biol. 2007 Feb;17(1):110-6. doi: 10.1016/j.sbi.2006.11.002. Epub 2006 Dec 6.
Bacterial transcription relies on the binding of dissociable sigma (sigma) factors to RNA polymerase (RNAP) for promoter specificity. The major variant sigma factor (sigma54) forms a stable closed complex with RNAP bound to DNA that rarely spontaneously isomerises to an open complex. ATP hydrolysis by bacterial enhancer-binding proteins is used to remodel the RNAP-sigma54-DNA closed complex. Recently, a wealth of structural information on bacterial enhancer-binding proteins has enabled unprecedented insights into their mechanism. These data provide a structural basis for nucleotide binding and hydrolysis, oligomerisation and the conversion of ATPase activity into remodelling events within the RNAP-sigma54 closed complex, and represent advances towards a complete understanding of the sigma54-dependent transcription activation mechanism.
细菌转录依赖于可解离的σ因子与RNA聚合酶（RNAP）结合以实现启动子特异性。主要的可变σ因子（σ54）与结合在DNA上的RNAP形成稳定的封闭复合物，该复合物很少自发异构化为开放复合物。细菌增强子结合蛋白的ATP水解用于重塑RNAP-σ54-DNA封闭复合物。最近，关于细菌增强子结合蛋白的大量结构信息使其机制得到了前所未有的深入了解。这些数据为核苷酸结合与水解、寡聚化以及ATP酶活性转化为RNAP-σ54封闭复合物内的重塑事件提供了结构基础，并代表了在全面理解σ54依赖性转录激活机制方面取得的进展。
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