ReviewBiophysics (Nagoya-shi, Japan)2011
The mechanism of protein export enhancement by the SecDF membrane component.
Review in Biophysics (Nagoya-shi, Japan), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- An RND transporter in the monoterpene metabolism of Castellaniella defragrans.Biodegradation · 2019Article
- Structural Basis for Cholesterol Transport-like Activity of the Hedgehog Receptor Patched.Cell · 2018Article
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2 authors.
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Abstract
Protein transport across membranes is a fundamental and essential cellular activity in all organisms. In bacteria, protein export across the cytoplasmic membrane, driven by dynamic interplays between the protein-conducting SecYEG channel (Sec translocon) and the SecA ATPase, is enhanced by the proton motive force (PMF) and a membrane-integrated Sec component, SecDF. However, the structure and function of SecDF have remained unclear. We solved the first crystal structure of SecDF, consisting of a pseudo-symmetrical 12-helix transmembrane domain and two protruding periplasmic domains. Based on the structural features, we proposed that SecDF functions as a membrane-integrated chaperone, which drives protein movement without using the major energetic currency, ATP, but with remarkable cycles of conformational changes, powered by the proton gradient across the membrane. By a series of biochemical and biophysical approaches, several functionally important residues in the transmembrane region have been identified and our model of the SecDF function has been verified.
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