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The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair

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Published copy (DOI)

Author(s)

  • Laura Manelyte
  • Colin P. Guy
  • Rachel M. Smith
  • Mark S. Dillingham
  • Peter McGlynn
  • Nigel J. Savery

Department/unit(s)

Publication details

JournalMutation research-Dna repair
DatePublished - 2 Nov 2009
Issue number11
Volume8
Number of pages11
Pages (from-to)1300-1310
Original languageEnglish

Abstract

During nucleotide excision repair (NER) in bacteria the UvrC nuclease and the short oligonucleotide that contains the DNA lesion are removed from the post-incision complex by UvrD, a superfamily 1A helicase. Helicases are frequently regulated by interactions with partner proteins, and immunoprecipitation experiments have previously indicated that UvrD interacts with UvrB, a component of the post-incision complex. We examined this interaction using 2-hybrid analysis and surface plasmon resonance spectroscopy, and found that the N-terminal domain and the unstructured region at the C-terminus of UvrD interact with UvrB. We analysed the properties of a truncated UvrD protein that lacked the unstructured C-terminal region and found that it showed a diminished affinity for single-stranded DNA, but retained the ability to displace both UvrC and the lesion-containing of oligonucleotide from a post-incision nucleotide excision repair complex. The interaction of the C-terminal region of UvrD with UvrB is therefore not an essential feature of the mechanism by which UvrD disassembles the post-incision complex during NER. In further experiments we showed that PcrA helicase from Bacillus stearothermophilus can also displace UvrC and the excised oligonucleotide from a post-incision NER complex, which supports the idea that PcrA performs a UvrD-like function during NER in Gram-positive organisms. (C) 2009 Elsevier B.V. All rights reserved.

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