ArticleProtein science : a publication of the Protein Society2010
Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
17 citing papers in PubMed.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- How SecB maintains clients in a translocation competent state.Communications biology · 2025Article
- Plastid Molecular Chaperone HSP90C Interacts with the SecA1 Subunit of Sec Translocase for Thylakoid Protein Transport.Plants (Basel, Switzerland) · 2024Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- 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
- 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 SecB-like chaperone Rv1957 from Mycobacterium tuberculosis: crystallization and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- Insights into the structure and assembly of Escherichia coli outer membrane protein A.The FEBS journal · 2012Review
- Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Applied and environmental microbiology · 2012Article
- Signal peptidase I: cleaving the way to mature proteins.Protein science : a publication of the Protein Society · 2012Review
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Energetics of SecA dimerization.Journal of molecular biology · 2011Article
- Orientation of SecA and SecB in complex, derived from disulfide cross-linking.Journal of bacteriology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Protein export mediated by the general secretory Sec system in Escherichia coli proceeds by a dynamic transfer of a precursor polypeptide from the chaperone SecB to the SecA ATPase motor of the translocon and subsequently into and through the channel of the membrane-embedded SecYEG heterotrimer. The complex between SecA and SecB is stabilized by several separate sites of contact. Here we have demonstrated directly an interaction between the N-terminal residues 2 through 11 of SecA and the C-terminal 13 residues of SecB by isothermal titration calorimetry and analytical sedimentation velocity centrifugation. We discuss the unusual binding properties of SecA and SecB in context of a model for transfer of the precursor along the pathway of export.
Indexed as
Identifiers
What OpenQuestion holds
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.