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. 1986 Sep 12;46(6):921-8. doi: 10.1016/0092-8674(86)90074-7.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

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

Substances

  • 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