Roles of SecG in ATP- and SecA-dependent protein translocation
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منابع مشابه
Roles of SecG in ATP- and SecA-dependent protein translocation.
SecA, the translocation ATPase in Escherichia coli, undergoes cycles of conformational changes (insertion/deinsertion) in response to ATP and a preprotein. The membrane-embedded portion of protein translocase, SecYEG, has crucial roles in the SecA-driven preprotein translocation reaction. We previously identified a secY mutation (secY205) that did not allow an ATP- and preprotein-dependent (pro...
متن کاملInversion of the Membrane Topology of SecG Coupled with SecA-Dependent Preprotein Translocation
E. coli preprotein translocase comprises SecA and SecY/E/G complex. SecA delivers the preprotein to the putative protein-conducting channel formed by SecY/E by undergoing ATP-driven cycles of membrane insertion and deinsertion. SecG renders the translocase highly efficient. An antibody raised against the C-terminal region of SecG inhibits preprotein translocation into everted membrane vesicles ...
متن کاملMultiple SecA molecules drive protein translocation across a single translocon with SecG inversion.
SecA is a translocation ATPase that drives protein translocation. D209N SecA, a dominant-negative mutant, binds ATP but is unable to hydrolyze it. This mutant was inactive to proOmpA translocation. However, it generated a translocation intermediate of 18 kDa. Further addition of wild-type SecA caused its translocation into either mature OmpA or another intermediate of 28 kDa that can be translo...
متن کاملReconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12).
A cytoplasmic membrane protein, p12, of Escherichia coli was discovered as a new factor that stimulates the protein translocation activity reconstituted with SecA, SecY, and SecE (Nishiyama, K., Mizushima, S., and Tokuda, H. (1993) EMBO J. 12, 3409-3415). Direct involvement of p12 in protein translocation was subsequently demonstrated in vivo by genetic studies, and the name SecG has been propo...
متن کاملA molecular switch in SecA protein couples ATP hydrolysis to protein translocation.
SecA, the dimeric ATPase subunit of bacterial protein translocase, catalyses translocation during ATP-driven membrane cycling at SecYEG. We now show that the SecA protomer comprises two structural modules: the ATPase N-domain, containing the nucleotide binding sites NBD1 and NBD2, and the regulatory C-domain. The C-domain binds to the N-domain in each protomer and to the C-domain of another pro...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.23.13567