Folding in vitro and transport in vivo of pre‐β‐lactamase are SecB independent
- 1 January 1991
- journal article
- Published by Wiley in Molecular Microbiology
- Vol. 5 (1) , 117-122
- https://doi.org/10.1111/j.1365-2958.1991.tb01832.x
Abstract
Summary: The rate of folding of the precursor of β‐lactamase is not influenced by the presence of SecB under conditions in which GroEL/ES retards the folding. Wild‐type β‐lactamase and several mutants in the signal or the mature protein, affecting either transport or enzyme kinetics and probably folding, were examined for total expression, total enzymatic activity, and transported β‐lactamase (in vivo resistance) in secB‐ and secB+ strains. We conclude that there is no indication of any relevant interaction between SecB and pre‐β‐lactamase in vitro, nor did the secB‐ mutation affect the transport of wild–type β‐lactamase or any of the mutants in vivo. Thus, putative Escherichia coli‘folding modulators’must be of limited specificity.Keywords
This publication has 40 references indexed in Scilit:
- No Specific Recognition of Leader Peptide by SecB, a Chaperone Involved in Protein ExportScience, 1990
- The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cellBiochemistry, 1990
- SecB functions as a cytosolic signal recognition factor for protein export in E. coliCell, 1989
- Transient association of newly synthesized unfolded proteins with the heat-shock GroEL proteinNature, 1988
- ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particleCell, 1988
- The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinCell, 1988
- Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin foldingBiochemistry, 1987
- Folding and association of proteinsProgress in Biophysics and Molecular Biology, 1987
- 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
- Binding of a specific ligand inhibits import of a purified precursor protein into mitochondriaNature, 1986