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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

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.

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