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

Research output: Contribution to journalArticle

Original languageEnglish
Article numbergkx074
Pages (from-to)3875-3887
Number of pages13
JournalNucleic Acids Research
Volume45
Issue number7
Early online date4 Feb 2017
DOIs
DateAccepted/In press - 18 Jan 2017
DateE-pub ahead of print - 4 Feb 2017
DatePublished (current) - 20 Apr 2017

Abstract

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.

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    Rights statement: This is the final published version of the article (version of record). It first appeared online via Oxford University Press at https://academic.oup.com/nar/article/2970149/The. Please refer to any applicable terms of use of the publisher.

    Final published version, 2.48 MB, PDF document

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  • Full-text PDF (final published version)

    Rights statement: This is the final published version of the article (version of record). It first appeared online via Oxford University Press at https://academic.oup.com/nar/article/45/7/3875/2970149 . Please refer to any applicable terms of use of the publisher.

    Final published version, 2.52 MB, PDF document

    Licence: CC BY

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