Sec-dependent preprotein translocation in bacteria
نویسندگان
چکیده
منابع مشابه
Sec-dependent membrane protein biogenesis: SecYEG, preprotein hydrophobicity and translocation kinetics control the stop-transfer function.
Preprotein translocase catalyzes membrane protein integration as well as complete translocation. Membrane proteins must interrupt their translocation and be laterally released from the translocase into the lipid bilayer. We have analyzed the translocation arrest and lateral release activities of Escherichia coli preprotein translocase with an in vitro reaction and the preprotein proOmpA carryin...
متن کاملEndogenous SecA catalyzes preprotein translocation at SecYEG.
SecA is found in the cytosol and bound to the plasma membrane of Escherichia coli. Binding occurs either with high affinity at SecYEG or with low affinity to lipid. Domains of 65 and 30 kDa of SecYEG-bound SecA insert into the membrane upon interaction with preprotein and ATP. Azide blocks preprotein translocation, in vivo and in vitro, through interacting with SecA and preventing SecA deinsert...
متن کاملCharged amino acids in a preprotein inhibit SecA-dependent protein translocation.
Sec translocase catalyzes membrane protein insertion and translocation. We have introduced stretches of charged amino acid residues into the preprotein proOmpA and have analyzed their effect on in vitro protein translocation into Escherichia coli inner membrane vesicles. Both negatively and positively charged amino acid residues inhibit translocation of proOmpA, yielding a partially translocate...
متن کاملDimeric SecA Couples the Preprotein Translocation in an Asymmetric Manner
The Sec translocase mediates the post-translational translocation of a number of preproteins through the inner membrane in bacteria. In the initiatory translocation step, SecB targets the preprotein to the translocase by specific interaction with its receptor SecA. The latter is the ATPase of Sec translocase which mediates the post-translational translocation of preprotein through the protein-c...
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 ...
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ژورنال
عنوان ژورنال: Archives of Microbiology
سال: 1996
ISSN: 0302-8933,1432-072X
DOI: 10.1007/s002030050289