ArticleJournal of molecular biology2011
Energetics of SecA dimerization.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- On the utility of fluorescence-detection analytical ultracentrifugation in probing biomolecular interactions in complex solutions: a case study in milk.European biophysics journal : EBJ · 2020Article
- Binding of SecA ATPase monomers and dimers to lipid vesicles.Biochimica et biophysica acta. Biomembranes · 2020Article
- Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.Protein science : a publication of the Protein Society · 2019Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Trk2 Potassium Transport System in Streptococcus mutans and Its Role in Potassium Homeostasis, Biofilm Formation, and Stress Tolerance.Journal of bacteriology · 2016Article
- A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.Structure (London, England : 1993) · 2015Article
- In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.PloS one · 2015Article
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1.The Journal of biological chemistry · 2014Article
- Mapping of the SecA signal peptide binding site and dimeric interface by using the substituted cysteine accessibility method.Journal of bacteriology · 2013Article
- Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking.Journal of bacteriology · 2013Article
- Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2013Article
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Heparin activates PKR by inducing dimerization.Journal of molecular biology · 2011Article
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
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Authors and funding
4 authors.
Funding
Abstract
Transport of many proteins to extracytoplasmic locations occurs via the general secretion (Sec) pathway. In Escherichia coli, this pathway is composed of the SecYEG protein-conducting channel and the SecA ATPase. SecA plays a central role in binding the signal peptide region of preproteins, directing preproteins to membrane-bound SecYEG and promoting translocation coupled with ATP hydrolysis. Although it is well established that SecA is crucial for preprotein transport and thus cell viability, its oligomeric state during different stages of transport remains ill defined. We have characterized the energetics of SecA dimerization as a function of salt concentration and temperature and defined the linkage of SecA dimerization and signal peptide binding using analytical ultracentrifugation. The use of a new fluorescence detector permitted an analysis of SecA dimerization down to concentrations as low as 50 nM. The dimer dissociation constants are strongly dependent on salt. Linkage analysis indicates that SecA dimerization is coupled to the release of about five ions, demonstrating that electrostatic interactions play an important role in stabilizing the SecA dimer interface. Binding of signal peptide reduces SecA dimerization affinity, such that K(d) increases about 9-fold from 0.28 μM in the absence of peptide to 2.68 μM in the presence of peptide. The weakening of the SecA dimer that accompanies signal peptide binding may poise the SecA dimer to dissociate upon binding to SecYEG.
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