ArticleJournal of molecular biology2015
The basis of asymmetry in the SecA:SecB complex.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- How SecB maintains clients in a translocation competent state.Communications biology · 2025Article
- Isolation and Characterization of a Novel Virulent Phage ASG01 ofMicroorganisms · 2024Article
- Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase.Viruses · 2021Article
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway.The protein journal · 2019Review
- Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.Journal of bacteriology · 2019Article
- secA, secD, secF, yajC, and yidC contribute to the adhesion regulation of Vibrio alginolyticus.MicrobiologyOpen · 2018Article
- 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 Sec System: Protein Export inEcoSal Plus · 2017Review
- SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport.Molecular microbiology · 2017Article
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
During export in Escherichia coli, SecB, a homotetramer structurally organized as a dimer of dimers, forms a complex with two protomers of SecA, which is the ATPase that provides energy to transfer a precursor polypeptide through the membrane via the SecYEG translocon. There are two areas of contact on SecB that stabilize the SecA:SecB complex: the flat sides of the SecB tetramer and the C-terminal 13 residues of SecB. These contacts within the complex are distributed asymmetrically. Breaking contact between SecA and the sides of SecB results in release of only one protomer of SecA yielding a complex of stoichiometry SecA1:SecB4. This complex mediates export; however, the coupling of ATP hydrolysis to movements of the precursor through the translocon is much less efficient than the coupling by the SecA2:SecB4 complex. Here we used heterotetrameric species of SecB to understand the source of the asymmetry in the contacts and its role in the functioning of the complex. The model of interactions presented suggests a way that binding between SecA and SecB might decrease the affinity of precursor polypeptides for SecB and facilitate the transfer to SecA.
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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.