Diverse Effects of Mutation on the Activity of the Escherichia coli Export Chaperone SecB
Open Access
- 1 September 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (39) , 22831-22835
- https://doi.org/10.1074/jbc.270.39.22831
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Determination of the binding frame within a physiological ligand for the chaperone SecBProtein Science, 1994
- Role of the Major Heat Shock Proteins as Molecular ChaperonesAnnual Review of Cell Biology, 1993
- Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivoJournal of Bacteriology, 1993
- Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative StructureScience, 1992
- DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.Genes & Development, 1992
- Molecular chaperones and protein translocation across the Escherichia coli inner membraneMolecular Microbiology, 1991
- Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.Proceedings of the National Academy of Sciences, 1988
- The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinCell, 1988
- Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coliCell, 1986
- BACTERIAL PERIPLASMIC TRANSPORT SYSTEMS: STRUCTURE, MECHANISM, AND EVOLUTIONAnnual Review of Biochemistry, 1986