Molecular chaperones and protein translocation across the Escherichia coli inner membrane
- 1 January 1991
- journal article
- review article
- Published by Wiley in Molecular Microbiology
- Vol. 5 (1), 19-22
- https://doi.org/10.1111/j.1365-2958.1991.tb01821.x
Abstract
Proteins that are able to translocate across biological membranes assume of loosely folded structure. In this review it is suggested that the loosely folded structure, referred to here as‘per‐folded conformation', is a particular structure that interacts favourably with components of the export apparatus. Two soluble factors, SecB and GroEL, have been implicated in maintenance of the pre‐folded conformation and have been termed‘molecular chaperones'. Results suggest that SecB may be a chaperone that is specialized for binding to exported protein precursors, while GroEL may be a general folding modulator that binds to many intracellular proteins.Keywords
This publication has 36 references indexed in Scilit:
- No Specific Recognition of Leader Peptide by SecB, a Chaperone Involved in Protein ExportScience, 1990
- Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coliNature, 1990
- Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATPNature, 1989
- Demonstration by genetic suppression of interaction of GroE products with many proteinsNature, 1989
- 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
- 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
- Binding of a specific ligand inhibits import of a purified precursor protein into mitochondriaNature, 1986
- Host participation in bacteriophage lambda head assemblyJournal of Molecular Biology, 1973