Biochemical Characterization of a Mutationally Altered Protein Translocase: Proton Motive Force Stimulation of the Initiation Phase of Translocation
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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.
The Dynamic SecYEG Translocon.
Oswald J, Njenga R, Natriashvili A, Sarmah P, Koch H Front Mol Biosci. 2021; 8:664241.
PMID: 33937339 PMC: 8082313. DOI: 10.3389/fmolb.2021.664241.
SecA-Mediated Protein Translocation through the SecYEG Channel.
Komarudin A, Driessen A Microbiol Spectr. 2019; 7(4).
PMID: 31373268 PMC: 10957188. DOI: 10.1128/microbiolspec.PSIB-0028-2019.
An energy transduction mechanism used in bacterial flagellar type III protein export.
Minamino T, Morimoto Y, Hara N, Namba K Nat Commun. 2011; 2:475.
PMID: 21934659 PMC: 3195256. DOI: 10.1038/ncomms1488.
Post-liberation cleavage of signal peptides is catalyzed by the site-2 protease (S2P) in bacteria.
Saito A, Hizukuri Y, Matsuo E, Chiba S, Mori H, Nishimura O Proc Natl Acad Sci U S A. 2011; 108(33):13740-5.
PMID: 21810987 PMC: 3158159. DOI: 10.1073/pnas.1108376108.
Boy D, Koch H Mol Biol Cell. 2009; 20(6):1804-15.
PMID: 19158385 PMC: 2655265. DOI: 10.1091/mbc.e08-08-0886.