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Journal of Bacteriology, January 2006, p. 335-338, Vol. 188, No. 1
0021-9193/06/$08.00+0     doi:10.1128/JB.188.1.335-338.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SecA Dimer Cross-Linked at Its Subunit Interface Is Functional for Protein Translocation

Lucia B. Jilaveanu and Donald Oliver*

Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, Connecticut 06459

Received 7 September 2005/ Accepted 6 October 2005

SecA facilitates protein transport across the eubacterial plasma membrane by its association with cargo proteins and the SecYEG translocon, followed by ATP-driven conformational changes that promote protein translocation in a stepwise manner. Whether SecA functions as a monomer or a dimer during this process has been the subject of considerable controversy. Here we utilize cysteine-directed mutagenesis along with the crystal structure of the SecA dimer to create a cross-linked dimer at its subunit interface, which was normally active for in vitro protein translocation.

* Corresponding author. Mailing address: Department of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459. Phone: (860) 685-3556. Fax: (860) 685-2141. E-mail: doliver{at}wesleyan.edu.

Journal of Bacteriology, January 2006, p. 335-338, Vol. 188, No. 1
0021-9193/06/$08.00+0     doi:10.1128/JB.188.1.335-338.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Das, S., Stivison, E., Folta-Stogniew, E., Oliver, D. (2008). Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State. J. Bacteriol. 190: 7302-7307 [Abstract] [Full Text]  
  • Wang, H., Na, B., Yang, H., Tai, P. C. (2008). Additional In Vitro and In Vivo Evidence for SecA Functioning as Dimers in the Membrane: Dissociation into Monomers Is Not Essential for Protein Translocation in Escherichia coli. J. Bacteriol. 190: 1413-1418 [Abstract] [Full Text]  
  • Gold, V. A. M., Robson, A., Clarke, A. R., Collinson, I. (2007). Allosteric Regulation of SecA: MAGNESIUM-MEDIATED CONTROL OF CONFORMATION AND ACTIVITY. J. Biol. Chem. 282: 17424-17432 [Abstract] [Full Text]  
  • Jilaveanu, L. B., Oliver, D. B. (2007). In Vivo Membrane Topology of Escherichia coli SecA ATPase Reveals Extensive Periplasmic Exposure of Multiple Functionally Important Domains Clustering on One Face of SecA. J. Biol. Chem. 282: 4661-4668 [Abstract] [Full Text]  
  • Mori, H., Ito, K. (2006). The Long {alpha}-Helix of SecA Is Important for the ATPase Coupling of Translocation. J. Biol. Chem. 281: 36249-36256 [Abstract] [Full Text]  
  • Mori, H., Ito, K. (2006). Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking. Proc. Natl. Acad. Sci. USA 103: 16159-16164 [Abstract] [Full Text]  


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