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PMID: 2202725 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Export of the periplasmic maltose-binding protein of Escherichia coli.

Journal of bioenergetics and biomembranes ·Vol. 22 ·No. 3 ·1990-06-00 ·Pages 401-39

Bassford PJ

Abstract

The export of the maltose-binding protein (MBP), the malE gene product, to the periplasm of Escherichia coli cells has been extensively investigated. The isolation of strains synthesizing MalE-LacZ hybrid proteins led to a novel genetic selection for mutants that accumulate export-defective precursor MBP (preMBP) in the cytoplasm. The export defects were subsequently shown to result from alterations in the MBP signal peptide. Analysis of these and a variety of mutants obtained in other ways has provided considerable insight into the requirements for an optimally functional MBP signal peptide. This structure has been shown to have multiple roles in the export process, including promoting entry of preMBP into the export pathway and initiating MBP translocation across the cytoplasmic membrane. The latter has been shown to be a late event relative to synthesis and can occur entirely posttranslationally, even many minutes after the completion of synthesis. Translocation requires that the MBP polypeptide exist in an export-competent conformation that most likely represents an unfolded state that is not inhibitory to membrane transit. The signal peptide contributes to the export competence of preMBP by slowing the rate at which the attached mature moiety folds. In addition, preMBP folding is thought to be further retarded by the binding of a cytoplasmic protein, SecB, to the mature moiety of nascent preMBP. In cells lacking this antifolding factor, MBP export represents a race between delivery of newly synthesized, export-competent preMBP to the translocation machinery in the cytoplasmic membrane and folding of preMBP into an export-incompetent conformation. SecB is one of three E. coli proteins classified as "molecular chaperones" by their ability to stabilize precursor proteins for membrane translocation.

MeSH Terms
ATP-Binding Cassette Transporters Amino Acid Sequence Bacterial Proteins/genetics,metabolism Base Sequence Biological Transport, Active Carrier Proteins/genetics,metabolism Escherichia coli/metabolism Escherichia coli Proteins Maltose-Binding Proteins Molecular Sequence Data Monosaccharide Transport Proteins Mutation Periplasmic Binding Proteins Protein Sorting Signals/genetics
Chemicals
ATP-Binding Cassette Transporters Bacterial Proteins Carrier Proteins Escherichia coli Proteins MalE protein, E coli Maltose-Binding Proteins Monosaccharide Transport Proteins Periplasmic Binding Proteins Protein Sorting Signals maltose transport system, E coli
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Bassford P J
Department of Microbiology and Immunology, School of Medicine, University of North Carolina, Chapel Hill 27599-7290.
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Article Info
Journal
Journal of bioenergetics and biomembranes
Abbr.
J Bioenerg Biomembr
ISSN
0145-479X
DOI
10.1007/BF00763175
Published
1990-06-00
Pages
401-39
Language
English
Region
United States
NLM ID
7701859
Subset
IM
Grants
NIAID NIH HHS · AI17292 · United States
External Links
PubMed source DOI: 10.1007/BF00763175 View journal details
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