NDLI: Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.

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Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Liu, Gseping Hardy, Simon J. S. Crane, Jennine M. Randall, Linda L.
Description	Country affiliation: United States Author Affiliation: Randall LL ( Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, Columbia, MO 65211, USA. liug@missouri.edu)
Abstract	SecB, a small tetrameric cytosolic chaperone in Escherichia coli, facilitates the export of precursor poly-peptides by maintaining them in a nonnative conformation and passing them to SecA, which is a peripheral member of the membrane-bound translocation apparatus. It has been proposed by several laboratories that as SecA interacts with various components along the export pathway, it undergoes conformational changes that are crucial to its function. Here we report details of molecular interactions between SecA and SecB, which may serve as conformational switches. One site of interaction involves the final C-terminal 21 amino acids of SecA, which are positively charged and contain zinc. The C terminus of each subunit of the SecA dimer makes contact with the flat beta-sheet that is formed by each dimer of the SecB tetramer. Here we demonstrate that a second interaction exists between the extreme C-terminal alpha-helix of SecB and a site on SecA, as yet undefined but different from the C terminus of SecA. We investigated the energetics of the interactions by titration calorimetry and characterized the hydrodynamic properties of complexes stabilized by both interactions or each interaction singly using sedimentation velocity centrifugation.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	13
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2004-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphatases Chemistry Metabolism Bacterial Proteins Bodily Secretions Membrane Transport Proteins Zinc Binding Sites Physiology Biological Transport Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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