ArticleBiochemistry2014
Analysis of SecA dimerization in solution.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Protein secretion zones during overexpression of amylase within the Gram-positive cell wall.BMC biology · 2023Article
- Topology of the SecA ATPase Bound to Large Unilamellar Vesicles.Journal of molecular biology · 2022Article
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Binding of SecA ATPase monomers and dimers to lipid vesicles.Biochimica et biophysica acta. Biomembranes · 2020Article
- Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles.Microorganisms · 2019Article
- Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.Protein science : a publication of the Protein Society · 2019Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- Protein translocation: what's the problem?Biochemical Society transactions · 2016Review
- Channel crossing: how are proteins shipped across the bacterial plasma membrane?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The Sec pathway mediates translocation of protein across the inner membrane of bacteria. SecA is a motor protein that drives translocation of preprotein through the SecYEG channel. SecA reversibly dimerizes under physiological conditions, but different dimer interfaces have been observed in SecA crystal structures. Here, we have used biophysical approaches to address the nature of the SecA dimer that exists in solution. We have taken advantage of the extreme salt sensitivity of SecA dimerization to compare the rates of hydrogen-deuterium exchange of the monomer and dimer and have analyzed the effects of single-alanine substitutions on dimerization affinity. Our results support the antiparallel dimer arrangement observed in one of the crystal structures of Bacillus subtilis SecA. Additional residues lying within the preprotein binding domain and the C-terminus are also protected from exchange upon dimerization, indicating linkage to a conformational transition of the preprotein binding domain from an open to a closed state. In agreement with this interpretation, normal mode analysis demonstrates that the SecA dimer interface influences the global dynamics of SecA such that dimerization stabilizes the closed conformation.
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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.