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Chapter 15 : The Structure of Bacterial RNA Polymerase

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The Structure of Bacterial RNA Polymerase, Page 1 of 2

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Abstract:

This chapter describes crystal structures of RNA polymerase (RNAP) structures and their implications for understanding the mechanism of transcription and the regulation of key steps in the transcription cycle. There are three main steps in the transcription cycle: initiation, elongation, and termination. The transcription elongation complex (TEC) is processive and extremely stable, transcribing at an average rate of 30 to 100 nucleotides for tens of kilobases down the DNA template. Much is known about the general architecture of RNAP and the nucleic acid scaffold in the TEC from biochemical experiments. The chapter provides a comprehensive overview of what has been learned from the bacterial RNAP structures and models. Rifampin positioned in binding pocket would block growth of the RNA chain past two or three nucleotides, explaining the bactericidal effect of the antibiotic. In the holoenzyme structure, two rearrangements in σ region 2 are evident. First, a loop that covers the core binding surface in region 2.2 moves out of the way. Second, the bundle of helices made up of regions 1.2 and 2.1 to 2.4 rotates about 12⁰ relative to the nonconserved region. The single-stranded RNA transcript in the RNA-exit channel has also been shown to be important for the stability of the elongation complex, possibly due to the flap domain closing down around the RNA. The publication of crystal structures for multiple forms of RNAP has made possible a much more detailed examination of the function of the enzyme and the mechanisms of catalysis, promoter recognition, and transcriptional activation.

Citation: Geszvain K, Landick R. 2005. The Structure of Bacterial RNA Polymerase, p 283-296. In Higgins N (ed), The Bacterial Chromosome. ASM Press, Washington, DC. doi: 10.1128/9781555817640.ch15

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