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

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, b

SUBMITTER: Manelyte L 

PROVIDER: S-EPMC2997466 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature