No Specific Recognition of Leader Peptide by SecB, a Chaperone Involved in Protein Export

Most proteins destined for export from Escherichia coli are made as precursors containing amino-terminal leader sequences that are essential for export and that are removed during the process. The initial step in export of a subset of proteins, which includes maltose-binding protein, is binding of t...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1990-05, Vol.248 (4957), p.860-863
Main Authors: Randall, L. L., Topping, T. B., Hardy, S. J. S.
Format: Article
Language:English
Subjects:
Affinity labeling
Amides
Amino acid sequence
Amino acid sequencing
Analysis
ATP-Binding Cassette Transporters
Bacterial Proteins - metabolism
Bacteriology
Binding Sites
Biological and medical sciences
Biological Transport
Biology
Carrier proteins
Carrier Proteins - metabolism
Chromatography
Chromosomes
Cytosol - metabolism
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
Immunosuppressants
Maltose-Binding Proteins
Microbiology
Molecular chaperones
Molecular Weight
Monosaccharide Transport Proteins
Permeability, membrane transport, intracellular transport
Physiological aspects
Protein binding
Protein Conformation
Protein precursors
Protein Precursors - metabolism
Protein refolding
Protein Sorting Signals - metabolism
Proteins
Sex chromosomes
T lymphocytes
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Summary:Most proteins destined for export from Escherichia coli are made as precursors containing amino-terminal leader sequences that are essential for export and that are removed during the process. The initial step in export of a subset of proteins, which includes maltose-binding protein, is binding of the precursor by the molecular chaperone SecB. This work shows directly that SecB binds with high affinity to unfolded maltose-binding protein but does not specifically recognize and bind the leader. Rather, the leader modulates folding to expose elements in the remainder of the polypeptide that are recognized by SecB.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2188362