Molecular chaperones and protein translocation across the Escherichia coli inner membrane.
Proteins that are able to translocate across biological membranes assume a loosely folded structure. In this review it is suggested that the loosely folded structure, referred to here as the 'pre-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.
Kumamoto
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CA
Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111.
D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D018834:Chaperonin 60; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism*
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D011498:Protein Precursors; C057842:SecB protein, Bacteria