Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, United States.
Curr Opin Struct Biol. 2009 Dec;19(6):708-14. doi: 10.1016/j.sbi.2009.10.008. Epub 2009 Nov 11.
The central role of RNA polymerase (RNAP) is to catalyze the processive synthesis of a growing RNA transcript. Recent structural and biophysical data have led to a deeper understanding of the nucleotide addition cycle and insight into the structure-function relationships that govern transcription elongation. In this review, we discuss kinetic data on nucleotide incorporation in the context of crystal structures, which show RNAP in multiple conformations. We present a facilitated Brownian ratchet model of nucleotide incorporation, in which templated NTP binding to a non-catalytic site in the main channel promotes the conformational changes that lead to opening of the catalytic site and translocation.
RNA 聚合酶(RNAP)的核心作用是催化不断延伸的 RNA 转录本的合成。最近的结构和生物物理数据使人们对核苷酸添加循环有了更深入的了解,并深入了解了控制转录延伸的结构-功能关系。在这篇综述中,我们将结合晶体结构讨论核苷酸掺入的动力学数据,这些结构显示了 RNAP 的多种构象。我们提出了核苷酸掺入的促进布朗棘轮模型,其中模板 NTP 结合到主通道中的非催化位点促进导致催化位点打开和易位的构象变化。