Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition
Open Access
- 1 January 1998
- journal article
- Published by Elsevier
- Vol. 273 (1) , 459-465
- https://doi.org/10.1074/jbc.273.1.459
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesPublished by Elsevier ,2004
- Communication of ClpXP protease hypersensitivity to bacteriophage mu repressor isoformsJournal of Molecular Biology, 1997
- ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.Genes & Development, 1997
- The mu transposase tetramer is inactive in unassisted strand transfer: an auto-allosteric effect of mu A promotes the reaction in the absence of mu BJournal of Molecular Biology, 1997
- Disassembly of the Mu transposase tetramer by the ClpX chaperone.Genes & Development, 1995
- Homology in Structural Organization BetweenE. coliClpAP Protease and the Eukaryotic 26 S ProteasomeJournal of Molecular Biology, 1995
- A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX proteinMolecular Microbiology, 1994
- Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: Implications for regulationCell, 1989
- Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancerNature, 1989
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976