SecB,one small chaperone in the complex milieu of the cell |
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Authors: | L L Randall S J S Hardy |
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Institution: | (1) Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, Missouri 65211 (USA), Fax +1 573 882 5635, US;(2) Department of Biology, University of York, PO Box 373, York YO10 5YW (United Kingdom), e-mail: sjsh1@york.ac.uk, GB |
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Abstract: | SecB is only one of a plethora of cytosolic chaperones in E. coli whose common property is that they bind nonnative proteins. It plays a crucial role during protein export via the general
secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound
translocation apparatus. In this latter role SecB demonstrates specific binding to a unique partner, SecA. SecB has the potential
to participate in functions outside of export acting as a general nonspecific chaperone to provide buffering capacity of the
nonnative state of proteins in the cytosolic pool. We discuss the interactions of SecB with its many binding partners in light
of its recently determined structure, emphasizing both kinetic and thermodynamic parameters.
RID="*"
ID="*"Corresponding author. |
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Keywords: | , Chaperone, SecB, export, secretion, |
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