Abstract:
:Export of protein into the periplasm of Escherichia coli via the general secretory system is achieved by action of a ternary complex comprising the polypeptide ligand, the chaperone SecB and SecA, a peripheral component of the membrane translocon, which is itself an ATPase. The unfolded ligand is captured initially by SecB and must be transferred to SecA and subsequently through the membrane translocon into the periplasm. We have taken the first steps in the elucidation of the mechanism of this dynamic transfer by determining the interface of interaction between SecB and SecA. Site-directed spin labeling and electron paramagnetic resonance spectroscopy were combined to identify which of the residues on SecB showed changes in spectral line shape upon addition of SecA. In all, 43% of the surface of SecB was covered by the 41 positions examined. A model of docking between SecB and SecA is proposed based on the pattern of amino acid residues on SecB shown to make contacts when in complex with SecA. This model in combination with previously published biochemical data provides insight into the transfer of the unfolded polypeptide from the chaperone SecB to SecA.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Crane JM,Mao C,Lilly AA,Smith VF,Suo Y,Hubbell WL,Randall LLdoi
10.1016/j.jmb.2005.08.022keywords:
subject
Has Abstractpub_date
2005-10-21 00:00:00pages
295-307issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(05)00959-9journal_volume
353pub_type
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