Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
http://academic.oup.com/nar/article-pdf/37/6/1962/18784055/gkp071.pdf
Reference27 articles.
1. ‘Close fitting sleeves’: DNA damage recognition by the UvrABC nuclease system;Van Houten;Mutat. Res.,2005
2. Prokaryotic nucleotide excision repair: the UvrABC system;Truglio;Chem. Rev.,2006
3. Crystal structure of UvrB, a DNA helicase adapted for nucleotide excision repair;Theis;EMBO J.,1999
4. The beta -hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions;Skorvaga;J. Biol. Chem.,2002
5. Structural basis for DNA recognition and processing by UvrB;Truglio;Nat. Struct. Mol. Biol.,2006
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