The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase

Emma J Gwynn, Abigail J Smith, Colin P Guy, Nigel J Savery, Peter McGlynn, Mark S Dillingham

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Abstract

UvrD-like helicases play diverse roles in DNA replication, repair and recombination pathways. An emerging body of evidence suggests that their different cellular functions are directed by interactions with partner proteins that target unwinding activity to appropriate substrates. Recent studies in E. coli have shown that UvrD can act as an accessory replicative helicase that resolves conflicts between the replisome and transcription complexes, but the mechanism is not understood. Here we show that the UvrD homologue PcrA interacts physically with B. subtilis RNA polymerase, and that an equivalent interaction is conserved in E. coli where UvrD, but not the closely related helicase Rep, also interacts with RNA polymerase. The PcrA-RNAP interaction is direct and independent of nucleic acids or additional mediator proteins. A disordered but highly conserved C-terminal region of PcrA, which distinguishes PcrA/UvrD from otherwise related enzymes such as Rep, is both necessary and sufficient for interaction with RNA polymerase.

Original languageEnglish
Article numbere78141
Number of pages11
JournalPloS ONE
Volume8
Issue number10
DOIs
Publication statusPublished - 16 Oct 2013

Keywords

  • couple DNA-repair
  • single-stranded-dna
  • stearothermophilus pcra helicase
  • Escherichia-coli
  • bacillus-subtilis
  • UVRD helicase
  • crystal-structures
  • structural basis
  • mismatch repair
  • in-vitro

Cite this

Gwynn, E. J., Smith, A. J., Guy, C. P., Savery, N. J., McGlynn, P., & Dillingham, M. S. (2013). The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase. PloS ONE, 8(10), [e78141]. https://doi.org/10.1371/journal.pone.0078141