The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase

Kelly Sanders, Chia Liang Lin, Abigail J. Smith, Nora Cronin, Gemma Fisher, Vasileios Eftychidis, Peter McGlynn, Nigel J. Savery, Dale B. Wigley, Mark S. Dillingham*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

19 Citations (Scopus)
273 Downloads (Pure)


The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1, 2) might be relevant to these functions, but the structural basis for this activity is poorly understood. In this work, we define a minimal RNA polymerase interaction domain in PcrA, and report its crystal structure at 1.5 Å resolution. The domain adopts a Tudorlike fold that is similar to other RNA polymerase interaction domains, including that of the prototype transcription-repair coupling factor Mfd. Removal or mutation of the interaction domain reduces the ability of PcrA/UvrD to interact with and to remodel RNA polymerase complexes in vitro. The implications of this work for our understanding of the role of PcrA/UvrD at the interface of DNA replication, transcription and repair are discussed.

Original languageEnglish
Article numbergkx074
Pages (from-to)3875-3887
Number of pages13
JournalNucleic Acids Research
Issue number7
Early online date4 Feb 2017
Publication statusPublished - 20 Apr 2017


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