ArticleJournal of bacteriology1998
Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.
Article in Journal of bacteriology, 1998. 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.
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- An experiment-informed signal transduction model for the role of the Staphylococcus aureus MecR1 protein in β-lactam resistance.Scientific reports · 2019Article
- 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
- Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase.Nature chemical biology · 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
- Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Fluorescein analogues inhibit SecA ATPase: the first sub-micromolar inhibitor of bacterial protein translocation.ChemMedChem · 2012Article
- SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.The Journal of biological chemistry · 2011Article
- The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: a possible general feature.Cellular & molecular biology letters · 2011Article
- The first low microM SecA inhibitors.Bioorganic & medicinal chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We have identified and characterized the protease-resistant SecA fragments (X. Chen, H. Xu, and P. C. Tai, J. Biol. Chem. 271:29698-29706, 1996) through immunodetection with region-specific antibodies, chemical extraction, and sequencing analysis. The 66-, 36-, and 27-kDa proteolytic fragments in the membranes all start at Met1, whereas the 48-kDa fragment starts at Glu361. The overlapping of the sequences of the 66- and 48-kDa fragments indicates that they are derived from different SecA molecules. These two fragments were generated differently in response to ATP hydrolysis and protein translocation. Furthermore, the presence of membrane is required for the generation of the 48-kDa fragment but not for that of the 66-kDa fragment. These data suggest that there are two different integral forms of SecA in the membrane: SecA(S) and SecA(M). The combination of these two forms of SecA has several membrane-interacting domains. Both forms of SecA are integrated in the membrane, since both the 48- and 66-kDa fragments could be derived from urea- or Na2CO3-washed membranes. Moreover, all fragments are resistant to extraction with a high concentration of salt or with heparin, but the membrane-specific 48-kDa SecA domain is more sensitive to Na2CO3 or urea extraction. This suggests that this domain may interact with other membrane proteins in an aqueous microenvironment and therefore may form a part of the protein-conducting channel.
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Registered trials
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