The bacterial Sec-translocase: structure and mechanism
نویسندگان
چکیده
منابع مشابه
The bacterial Sec-translocase: structure and mechanism.
Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP-dependent motor protein SecA. The ancillary SecDF membrane protein complex promotes the final stages of translocation. Recent years have seen a major advance in our understanding of the structural and biochemical basis of protein translocat...
متن کاملBacterial sec-translocase unfolds and translocates a class of folded protein domains.
It is generally assumed that preprotein substrates must be presented in an unfolded state to the bacterial Sec-translocase in order to be translocated. Here, we have examined the ability of the Sec-translocase to translocate folded preproteins. Tightly folded human cardiac Ig-like domain I27 fused to the C terminus of proOmpA is translocated efficiently by the Sec-translocase and the translocat...
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15 صفحه اولUniversity of Groningen The bacterial sec machinery
It has been proposed that the bitopic membrane protein SecG undergoes topology inversion during translocation of (pre)proteins via SecYEG. Here we show that SecG covalently cross-linked to SecY cannot invert its topology while remaining fully functional in protein translocation. Our results strongly disfavor topology inversion of SecG during protein translocation.
متن کاملBacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme.
Preprotein translocase, the membrane transporter for secretory proteins, is a processive enzyme. It comprises the membrane proteins SecYEG(DFYajC) and the peripheral ATPase SecA, which acts as a motor subunit. Translocase subunits form dynamic complexes in the lipid bilayer and build an aqueous conduit through which preprotein substrates are transported at the expense of energy. Preproteins bin...
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ژورنال
عنوان ژورنال: Philosophical Transactions of the Royal Society B: Biological Sciences
سال: 2012
ISSN: 0962-8436,1471-2970
DOI: 10.1098/rstb.2011.0201