ArticleJournal of bacteriology2006
Archaeal and bacterial SecD and SecF homologs exhibit striking structural and functional conservation.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Review
- Article
- The very early evolution of protein translocation across membranes.PLoS computational biology · 2021Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor.FEMS microbiology letters · 2018Review
- secA, secD, secF, yajC, and yidC contribute to the adhesion regulation of Vibrio alginolyticus.MicrobiologyOpen · 2018Article
- Differential Protein Expression During Growth on Medium Versus Long-Chain Alkanes in the Obligate Marine Hydrocarbon-Degrading BacteriumFrontiers in microbiology · 2018Article
- Electric-Field-Induced Protein Translocation via a Conformational Transition in SecDF: An MD Study.Biophysical journal · 2017Article
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- Autocatalytic maturation of the Tat-dependent halophilic subtilase Nep produced by the archaeon Natrialba magadii.Journal of bacteriology · 2012Article
- Article
- The mechanism of protein export enhancement by the SecDF membrane component.Biophysics (Nagoya-shi, Japan) · 2011Review
- Shaping the archaeal cell envelope.Archaea (Vancouver, B.C.) · 2010Review
- Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion.Journal of bacteriology · 2010Article
- Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of secretory proteins are translocated into and across hydrophobic membranes via the universally conserved Sec pore. Accessory proteins, including the SecDF-YajC Escherichia coli membrane complex, are required for efficient protein secretion. E. coli SecDF-YajC has been proposed to be involved in the membrane cycling of SecA, the cytoplasmic bacterial translocation ATPase, and in the stabilizing of SecG, a subunit of the Sec pore. While there are no identified archaeal homologs of either SecA or SecG, many archaea possess homologs of SecD and SecF. Here, we present the first study that addresses the function of archaeal SecD and SecF homologs. We show that the SecD and SecF components in the model archaeon Haloferax volcanii form a cytoplasmic membrane complex in the native host. Furthermore, as in E. coli, an H. volcanii deltasecFD mutant strain exhibits both severe cold sensitivity and a Sec-specific protein translocation defect. Taken together, these results demonstrate significant functional conservation among the prokaryotic SecD and SecF homologs despite the distinct composition of their translocation machineries.
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