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Binding, Activation and Dissociation of the Dimeric SecA ATPase at the Dimeric SecYEG Translocase

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Journal EMBO J
Date 2003 Aug 28
PMID 12941690
Citations 61
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Abstract

The bacterial preprotein translocase is comprised of a membrane-embedded oligomeric SecYEG structure and a cytosolic dimeric SecA ATPase. The associations within SecYEG oligomers and SecA dimers, as well as between these two domains are dynamic and reversible. Here, it is shown that a covalently linked SecYEG dimer forms a functional translocase and a high affinity binding site for monomeric and dimeric SecA in solution. The interaction between these two domains stimulates the SecA ATPase, and nucleotides modulate the affinity and ratio of SecA monomers and dimers bound to the linked SecYEG complex. During the translocation reaction, the SecA monomer remains in stable association with a SecYEG protomer and the translocating preprotein. The nucleotides and translocation-dependent changes of SecA-SecYEG associations and the SecA dimeric state may reflect important facets of the preprotein translocation reaction.

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References
1.
Manting E, van der Does C, Remigy H, Engel A, Driessen A . SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 2000; 19(5):852-61. PMC: 305625. DOI: 10.1093/emboj/19.5.852. View

2.
Matsumoto G, Yoshihisa T, Ito K . SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane. EMBO J. 1997; 16(21):6384-93. PMC: 1170245. DOI: 10.1093/emboj/16.21.6384. View

3.
van der Wolk J, Fekkes P, Boorsma A, Huie J, Silhavy T, Driessen A . PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation. EMBO J. 1998; 17(13):3631-9. PMC: 1170699. DOI: 10.1093/emboj/17.13.3631. View

4.
Shilton B, Svergun D, Volkov V, Koch M, Cusack S, Economou A . Escherichia coli SecA shape and dimensions. FEBS Lett. 1998; 436(2):277-82. DOI: 10.1016/s0014-5793(98)01141-7. View

5.
Meyer T, Menetret J, Breitling R, Miller K, Akey C, Rapoport T . The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J Mol Biol. 1999; 285(4):1789-800. DOI: 10.1006/jmbi.1998.2413. View