Roles of zinc-binding domain of bacterial RNA polymerase in transcription

Yangbo Hu, Bin Liu

Research output: Contribution to journalReview articlepeer-review

7 Scopus citations

Abstract

Transcription is an essential and multistep process carried out by RNA polymerase (RNAP). In bacterial RNAP, in addition to the catalytic core domain, multiple other conserved domains are also identified to play regulatory roles in transcription. One such domain is the zinc-binding domain (ZBD) located at the N terminus of the largest subunit β′ in bacterial RNAP, whose homolog is also reported in eukaryotic RNAPs. Recent structural and biochemical studies have revealed various key roles of the conserved β′ ZBD during different steps of transcription. In this review, we summarize recent progress on the regulatory roles of this β′ ZBD in bacterial transcription.

Original languageEnglish (US)
Pages (from-to)710-724
Number of pages15
JournalTrends in Biochemical Sciences
Volume47
Issue number8
DOIs
StatePublished - Aug 2022

Bibliographical note

Funding Information:
We thank Y. Yang at the Iowa State University for his critical reading of the manuscript. Y. H. is supported by National Natural Science Foundation of China [ 31870133 ], National Key R&D Program of China ( 2021YFA1300901 ) and the Young Top-notch Talent Cultivation Program of Hubei Province. B. L. is supported by Start-up funding from The Hormel Institute, University of Minnesota .

Publisher Copyright:
© 2022 The Author(s)

Keywords

  • elongation
  • recycling
  • termination and antitermination
  • transcription initiation
  • transcriptional regulation
  • transcription–translation coupling

PubMed: MeSH publication types

  • Journal Article
  • Review
  • Research Support, Non-U.S. Gov't

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