RNA Polymerase Structure, Bacterial

Research output: Chapter in Book/Report/Conference proceedingChapter

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Abstract

The multisubunit DNA-dependent RNA polymerase (RNAP) mediates transcription - the first step in gene expression in all cellular organisms. Its basic function is to faithfully synthesize an RNA chain complementary to the transcribed (template) DNA strand in the presence of substrates, ribonucleoside 5'-triphosphates. RNAP structure and function are highly conserved in all three kingdoms of life: bacteria, archaea, and eukaryotes. In bacteria and archaea, a single RNAP enzyme is responsible for the synthesis of all RNAs in the cell, including messenger RNA, ribosomal RNA, transfer RNA, and small noncoding RNA. In eukaryotes, these functions are divided between three related nuclear RNAPs. To orchestrate transcription of ~4000 bacterial genes during cell growth and in response to environmental signals, the enzymatic activity of RNAP is tightly regulated by both intrinsic signals (in DNA template and nascent RNA) and various extrinsic factors (proteins, short peptides, noncoding RNAs, and some small molecules). Extensive genetic, biochemical, and structural studies of RNAP and its regulatory factors conducted in the past 15 years have greatly expanded our knowledge of the organization and function of all major elements of transcription machinery. This article provides a summary of our current understanding of the structure and the mechanisms of action of bacterial RNAPs.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Pages173-184
Number of pages12
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
DOIs
StatePublished - Feb 15 2013

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All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Borukhov, S. (2013). RNA Polymerase Structure, Bacterial. In Encyclopedia of Biological Chemistry: Second Edition (pp. 173-184). Elsevier Inc.. https://doi.org/10.1016/B978-0-12-378630-2.00265-6