ArticleJournal of molecular biology2006
Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
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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
26 citing papers in PubMed.
- How SecB maintains clients in a translocation competent state.Communications biology · 2025Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Structural insights into chaperone addiction of toxin-antitoxin systems.Nature communications · 2019Article
- Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.Journal of bacteriology · 2019Article
- Bacterial secretion chaperones: the mycobacterial type VII case.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
- Directed evolution of SecB chaperones toward toxin-antitoxin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Chaperone addiction of toxin-antitoxin systems.Nature communications · 2016Article
- Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Biochemistry · 2016Article
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- Multitasking SecB chaperones in bacteria.Frontiers in microbiology · 2014Review
- Characterization of the secretion pathway of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2012Article
- Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy.PloS one · 2012Article
- 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
- Integrating protein homeostasis strategies in prokaryotes.Cold Spring Harbor perspectives in biology · 2011Review
- Orientation of SecA and SecB in complex, derived from disulfide cross-linking.Journal of bacteriology · 2011Article
- Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.Journal of biomolecular NMR · 2010Article
- Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Export of protein into the periplasm of Escherichia coli via the general secretory system requires that the transported polypeptides be devoid of stably folded tertiary structure. Capture of the precursor polypeptides before they fold is achieved by the promiscuous binding to the chaperone SecB. SecB delivers its ligand to export sites through its specific binding to SecA, a peripheral component of the membrane translocon. At the translocon the ligand is passed from SecB to SecA and subsequently through the SecYEG channel. We have previously used site-directed spin labeling and electron paramagnetic resonance spectroscopy to establish a docking model between SecB and SecA. Here we report use of the same strategy to map the pathway of a physiologic ligand, the unfolded form of precursor galactose-binding protein, on SecB. Our set of SecB variants each containing a single cysteine, which was used in the previous study, has been expanded to 48 residues, which cover 49% of the surface of SecB. The residues on SecB involved in contacts were identified as those that, upon addition of the unfolded polypeptide ligand, showed changes in spectral line shape consistent with restricted motion of the nitroxide. We conclude that the bound precursor makes contact with a large portion of the surface of the small chaperone. The sites on SecB that interact with the ligand are compared with the previously identified sites that interact with SecA and a model for transfer of the ligand is discussed.
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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.