ArticleThe Journal of biological chemistry2011
SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- Bacteria-Responsive Nanostructured Drug Delivery Systems for Targeted Antimicrobial Therapy.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Article
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.Protein science : a publication of the Protein Society · 2018Article
- The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.The Journal of biological chemistry · 2017Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Article
- Using Chemical Probes to Assess the Feasibility of Targeting SecA for Developing Antimicrobial Agents against Gram-Negative Bacteria.ChemMedChem · 2016Article
- Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors.ChemMedChem · 2016Article
- Evaluation of small molecule SecA inhibitors against methicillin-resistant Staphylococcus aureus.Bioorganic & medicinal chemistry · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities.Biochemical and biophysical research communications · 2014Article
- The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities.Biochemical and biophysical research communications · 2014Article
- SecAAA trimer is fully functional as SecAA dimer in the membrane: existence of higher oligomers?Biochemical and biophysical research communications · 2014Article
- Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome.The Journal of biological chemistry · 2014Article
- Differential expression of secretion machinery during bacterial growth: SecY and SecF decrease while SecA increases during transition from exponential phase to stationary phase.Current microbiology · 2013Article
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins.The Journal of membrane biology · 2013Article
- Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
SecA is an essential component of the Sec-dependent protein translocation pathway across cytoplasmic membranes in bacteria. Escherichia coli SecA binds to cytoplasmic membranes at SecYEG high affinity sites and at phospholipid low affinity sites. It has been widely viewed that SecYEG functions as the essential protein-conducting channel through which precursors cross the membranes in bacterial Sec-dependent pathways, and that SecA functions as a motor to hydrolyze ATP in translocating precursors through SecYEG channels. We have now found that SecA alone can promote precursor translocation into phospholiposomes. Moreover, SecA-liposomes elicit ionic currents in Xenopus oocytes. Patch-clamp recordings further show that SecA alone promotes signal peptide- or precursor-dependent single channel activity. These activities were observed with the functional SecA at about 1-2 μM. The results show that SecA alone is sufficient to promote protein translocation into liposomes and to elicit ionic channel activity at the phospholipids low affinity binding sites, thus indicating that SecA is able to form the protein-conducting channels. Even so, such SecA-liposomes are less efficient than those with a full complement of Sec proteins, and lose the signal-peptide proofreading function, resembling the effects of PrlA mutations. Addition of purified SecYEG restores the signal peptide specificity and increases protein translocation and ion channel activities. These data show that SecA can promote protein translocation and ion channel activities both when it is bound to lipids at low affinity sites and when it is bound to SecYEG with high affinity. The latter of the two interactions confers high efficiency and specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.