Download MendeleyThe structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase.
Sanders, K., Lin, C.L., Smith, A.J., Cronin, N., Fisher, G., Eftychidis, V., McGlynn, P., Savery, N.J., Wigley, D.B., Dillingham, M.S.(2017) Nucleic Acids Res 45: 3875-3887
- PubMed: 28160601
- DOI: https://doi.org/10.1093/nar/gkx074
- Primary Citation of Related Structures:
5DMA - PubMed 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 Tudor-like 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.
Organizational Affiliation:
DNA:Protein Interactions Unit, School of Biochemistry, Biomedical Sciences Building, University of Bristol, Bristol BS8 1TD, UK.
