Covalently dimerized SecA is functional in protein translocation - PubMed (original) (raw)
. 2005 Oct 21;280(42):35255-60.
doi: 10.1074/jbc.M506157200. Epub 2005 Aug 22.
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- PMID: 16115882
- DOI: 10.1074/jbc.M506157200
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Covalently dimerized SecA is functional in protein translocation
Jeanine de Keyzer et al. J Biol Chem. 2005.
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Abstract
The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein translocation is a topic of debate. To study the requirements of oligomeric changes in SecA during protein translocation, a non-dissociable SecA dimer was formed by oxidation of the carboxyl-terminal cysteines. The cross-linked SecA dimer interacts with the SecYEG complex with a similar stoichiometry as non-cross-linked SecA. Cross-linking reversibly disrupts the SecB binding site on SecA. However, in the absence of SecB, the activity of the disulfide-bonded SecA dimer is indistinguishable from wild-type SecA. Moreover, SecYEG binding stabilizes a cold sodium dodecylsulfate-resistant dimeric state of SecA. The results demonstrate that dissociation of the SecA dimer is not an essential feature of the protein translocation reaction.
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