ArticleThe Journal of membrane biology2006
Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels.
Article in The Journal of membrane biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The trial behind it
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- 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
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Article
- Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity.The Journal of membrane biology · 2012Article
- SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein translocation in Escherichia coli requires protein-conducting channels in cytoplasmic membranes to allow precursor peptides to pass through with adenosine triphosphate (ATP) hydrolysis. Here, we report a novel, sensitive method that detects the opening of the SecA-dependent protein-conducting channels at the nanogram level. E. coli inverted membrane vesicles were injected into Xenopus oocytes, and ionic currents were recorded using the two-electrode voltage clamp. Currents were observed only in the presence of E. coli SecA in conjunction with E. coli membranes. Observed currents showed outward rectification in the presence of KCl as permeable ions and were significantly enhanced by coinjection with the precursor protein proOmpA or active LamB signal peptide. Channel activity was blockable with sodium azide or adenylyl 5'-(beta,gamma-methylene)-diphosphonate, a nonhydrolyzable ATP analogue, both of which are known to inhibit SecA protein activity. Endogenous oocyte precursor proteins also stimulated ion current activity and can be inhibited by puromycin. In the presence of puromycin, exogenous proOmpA or LamB signal peptides continued to enhance ionic currents. Thus, the requirement of signal peptides and ATP hydrolysis for the SecA-dependent currents resembles biochemical protein translocation assay with E. coli membrane vesicles, indicating that the Xenopus oocyte system provides a sensitive assay to study the role of Sec and precursor proteins in the formation of protein-conducting channels using electrophysiological methods.
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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.