An Essential Role for the DnaK Molecular Chaperone in Stabilizing Over-expressed Substrate Proteins of the Bacterial Twin-arginine Translocation Pathway
- 30 March 2007
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 367 (3) , 715-730
- https://doi.org/10.1016/j.jmb.2007.01.027
Abstract
No abstract availableKeywords
This publication has 82 references indexed in Scilit:
- X-ray structure of a protein-conducting channelNature, 2003
- The structural basis of protein targeting and translocation in bacteria.Nature Structural & Molecular Biology, 2001
- Substrate Specificity of the SecB ChaperoneJournal of Biological Chemistry, 1999
- Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coliJournal of Bacteriology, 1996
- DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.Genes & Development, 1992
- Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coliNature, 1990
- Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.Proceedings of the National Academy of Sciences, 1989
- Escherichia coli SecB protein associates with exported protein precursors in vivo.Proceedings of the National Academy of Sciences, 1989
- Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB.Proceedings of the National Academy of Sciences, 1989
- The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinCell, 1988