Unique Contacts Direct High-Priority Recognition of the Tetrameric Mu Transposase-DNA Complex by the AAA+ Unfoldase ClpX
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology
Reference49 articles.
1. ATP-dependent proteases of bacteria: recognition logic and operating principles;Baker;Trends Biochem. Sci.,2006
2. MuB protein allosterically activates strand transfer by the transposase of phage Mu;Baker;Cell,1991
3. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins;Barnett;J. Biol. Chem.,2005
4. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study;Bolon;Mol. Cell,2004
5. Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex;Burton;Chem. Biol.,2003
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