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PMID: 3530497 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli.

Cell ·Vol. 46 ·No. 6 ·1986-09-12 ·Pages 921-8

Randall LL, Hardy SJ

Abstract

Sensitivity to proteolytic degradation was used to monitor folding of polypeptides in vivo. A correlation between competence for export and lack of stable tertiary structure was established by comparing the kinetics of folding of mutated precursor maltose-binding protein that carries a defective leader peptide with the kinetics of folding of wild-type precursor that is competent for export. It is proposed that during export a kinetic competition exists between productive translocation and folding of precursor intracellularly into a stable conformation that is not compatible with transfer.

MeSH Terms
ATP-Binding Cassette Transporters Bacterial Proteins/metabolism Biological Transport Carrier Proteins/metabolism Cell Compartmentation Endopeptidase K Endopeptidases Escherichia coli Escherichia coli Proteins Kinetics Maltose-Binding Proteins Membrane Proteins/metabolism Monosaccharide Transport Proteins Protein Conformation Protein Processing, Post-Translational Structure-Activity Relationship
Chemicals
ATP-Binding Cassette Transporters Bacterial Proteins Carrier Proteins Escherichia coli Proteins Maltose-Binding Proteins Membrane Proteins Monosaccharide Transport Proteins maltose transport system, E coli Endopeptidases Endopeptidase K
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Randall L L
Hardy S J
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1986-09-12
Pages
921-8
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Grants
NIGMS NIH HHS · GM29798 · United States
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