ArticleThe EMBO journal1997
The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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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.
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Who cites it
67 citing papers in PubMed, 191 citations in OpenAlex.
- Article
- Mutations that confer resistance to sodium azide affect the levels of two physiological isoforms of SecA inMicrobiology (Reading, England) · 2026Article
- Article
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Iron is a ligand of SecA-like metal-binding domainsThe Journal of biological chemistry · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Protein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria.Microbiology spectrum · 2019Review
- Article
- Genetic Analysis of Protein Translocation.The protein journal · 2019Review
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.PloS one · 2017Article
- Protein translocation: what's the problem?Biochemical Society transactions · 2016Review
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Article
- Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Chemical reviews · 2014Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chaperone SecB keeps precursor proteins in a translocation-competent state and targets them to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli. SecA is thought to recognize SecB via its carboxy-terminus. To determine the minimal requirement for a SecB-binding site, fusion proteins were created between glutathione-S-transferase and different parts of the carboxy-terminus of SecA and analysed for SecB binding. A strikingly short amino acid sequence corresponding to only the most distal 22 aminoacyl residues of SecA suffices for the authentic binding of SecB or the SecB-precursor protein complex. SecAN880, a deletion mutant that lacks this highly conserved domain, still supports precursor protein translocation but is unable to bind SecB. Heterodimers of wild-type SecA and SecAN880 are defective in SecB binding, demonstrating that both carboxy-termini of the SecA dimer are needed to form a genuine SecB-binding site. SecB is released from the translocase at a very early stage in protein translocation when the membrane-bound SecA binds ATP to initiate translocation. It is concluded that the SecB-binding site on SecA is confined to the extreme carboxy-terminus of the SecA dimer, and that SecB is released from this site at the onset of translocation.
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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.