ArticleProceedings of the National Academy of Sciences of the United States of America1997
Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 80 citations in OpenAlex.
- Evolutionary evidence on suitability of SecD as a target for development of antibacterial agents against Staphylococcus aureus.Ecology and evolution · 2016Article
- Sec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteria.Biochimica et biophysica acta · 2014Review
- ATPase active-site electrostatic interactions control the global conformation of the 100 kDa SecA translocase.Journal of the American Chemical Society · 2013Article
- Article
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.The Journal of biological chemistry · 2012Article
- Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.The Journal of biological chemistry · 2011Article
- Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.Molecular biology of the cell · 2009Article
- Assembly of the translocase motor onto the preprotein-conducting channel.Molecular microbiology · 2008Article
- Preprotein-controlled catalysis in the helicase motor of SecA.The EMBO journal · 2007Article
- Cross-linked SecA dimers are not functional in protein translocation.FEBS letters · 2007Article
- Probing the affinity of SecA for signal peptide in different environments.Biochemistry · 2005Article
- Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.The Journal of biological chemistry · 2005Article
- Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study.Journal of molecular biology · 2003Article
- Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase.The EMBO journal · 2003Article
- The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure.The EMBO journal · 2002Article
- Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome.Microbiology and molecular biology reviews : MMBR · 2000Review
- Evaluating the oligomeric state of SecYEG in preprotein translocase.The EMBO journal · 2000Article
- Role of lipids in the translocation of proteins across membranes.The Biochemical journal · 2000Review
- SecYEG assembles into a tetramer to form the active protein translocation channel.The EMBO journal · 2000Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SecA, a 102-kDa hydrophilic protein, couples the energy of ATP binding to the translocation of preprotein across the bacterial inner membrane. SecA function and topology were studied with metabolically labeled [35S]SecA and with inner membrane vesicles from cells that overexpressed SecYEGDFyajC, the integral domain of preprotein translocase. During translocation in the presence of ATP and preprotein, a 65-kDa N-terminal domain of SecA is protected from proteolytic digestion through insertion into the membrane, as previously reported for a 30-kDa C-terminal domain [Economou, A. & Wickner, W. (1994) Cell 78, 835-843]. Insertion of both domains occurs at saturable SecYEGDFyajC sites and is rapidly followed by deinsertion. SecA also associates nonsaturably and unproductively with lipid. In the presence of ATP, yet without involvement of preprotein or SecYEG, lipid-bound SecA forms domains that are protease-resistant and that remain so even upon subsequent membrane disruption. Unlike the [35S]SecA that inserts into the membrane at SecYEGDFyajC as it promotes preprotein translocation, lipid-associated [35S]SecA does not chase from its protease-resistant state upon the addition of excess SecA. The finding that two domains of SecA (which together represent most regions of the polypeptide chain) cycle into the membrane during preprotein translocation, as well as the distinction between the membrane association of SecA at translocation sites of SecYEGDFyajC and at nonproductive lipid sites, are fundamental to the study of the role of SecA in preprotein movement.
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