Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.1901.pdf
Reference36 articles.
1. Dillingham, M.S. & Kowalczykowski, S.C. RecBCD enzyme and the repair of double-stranded DNA breaks. Microbiol. Mol. Biol. Rev. 72, 642–671 (2008).
2. Singleton, M.R., Dillingham, M.S. & Wigley, D.B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76, 23–50 (2007).
3. Dillingham, M.S., Spies, M. & Kowalczykowski, S.C. RecBCD enzyme is a bipolar DNA helicase. Nature 423, 893–897 (2003).
4. Taylor, A.F. & Smith, G.R. RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature 423, 889–893 (2003).
5. Rigden, D.J. An inactivated nuclease-like domain in RecC with novel function: implications for evolution. BMC Struct. Biol. 5, 9 (2005).
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