ArticleBiochemistry2010
Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features.Journal of visualized experiments : JoVE · 2022Article
- The Structure ofInternational journal of molecular sciences · 2020Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Biochemistry · 2016Article
- Identification of small-molecule inhibitors against SecA by structure-based virtual ligand screening.The Journal of antibiotics · 2015Article
- A starting point for fluorescence-based single-molecule measurements in biomolecular research.Molecules (Basel, Switzerland) · 2014Review
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Proteins · 2014Article
- Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2013Article
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- Emerging themes in SecA2-mediated protein export.Nature reviews. Microbiology · 2012Review
- A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.The Journal of biological chemistry · 2012Article
- The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release.Journal of bacteriology · 2012Article
- Using a low denaturant model to explore the conformational features of translocation-active SecA.Biochemistry · 2012Article
- Characterization of the Escherichia coli SecA signal peptide-binding site.Journal of bacteriology · 2012Article
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Authors and funding
6 authors.
Funding
Abstract
Identification of the signal peptide-binding domain within SecA ATPase is an important goal for understanding the molecular basis of SecA preprotein recognition as well as elucidating the chemo-mechanical cycle of this nanomotor during protein translocation. In this study, Forster resonance energy transfer methodology was employed to map the location of the SecA signal peptide-binding domain using a collection of functional monocysteine SecA mutants and alkaline phosphatase signal peptides labeled with appropriate donor-acceptor fluorophores. Fluorescence anisotropy measurements yielded an equilibrium binding constant of 1.4 or 10.7 muM for the alkaline phosphatase signal peptide labeled at residue 22 or 2, respectively, with SecA, and a binding stoichiometry of one signal peptide bound per SecA monomer. Binding affinity measurements performed with a monomer-biased mutant indicate that the signal peptide binds equally well to SecA monomer or dimer. Distance measurements determined for 13 SecA mutants show that the SecA signal peptide-binding domain encompasses a portion of the preprotein cross-linking domain but also includes regions of nucleotide-binding domain 1 and particularly the helical scaffold domain. The identified region lies at a multidomain interface within the heart of SecA, surrounded by and potentially responsive to domains important for binding nucleotide, mature portions of the preprotein, and the SecYEG channel. Our FRET-mapped binding domain, in contrast to the domain identified by NMR spectroscopy, includes the two-helix finger that has been shown to interact with the preprotein during translocation and lies at the entrance to the protein-conducting channel in the recently determined SecA-SecYEG structure.
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