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Journal of Bacteriology, January 2003, p. 405-412, Vol. 185, No. 2
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.2.405-412.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Biochemical Characterization of a Mutationally Altered Protein Translocase: Proton Motive Force Stimulation of the Initiation Phase of Translocation

Hiroyuki Mori and Koreaki Ito*

Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan

Received 15 July 2002/ Accepted 21 October 2002

Protein translocation across the Escherichia coli plasma membrane is facilitated by concerted actions of the SecYEG integral membrane complex and the SecA ATPase. A secY mutation (secY39) affects Arg357, an evolutionarily conserved and functionally important residue, and impairs the translocation function in vivo and in vitro. In this study, we used the "superactive" mutant forms of SecA, which suppress the SecY39 deficiency, to characterize the mutationally altered SecY39EG translocase. It was found that SecY39-mediated preprotein translocation exhibited absolute dependence on the proton motive force. The proton motive force-dependent step proved to lie before signal peptide cleavage. We suggest that the proton motive force assists in the initiation phase of protein translocation.

* Corresponding author. Mailing address: Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan. Phone: 81 75 751 4015. Fax: 81 75 771 5699. E-mail: kito{at}virus.kyoto-u.ac.jp.

Journal of Bacteriology, January 2003, p. 405-412, Vol. 185, No. 2
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.2.405-412.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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