ArticleBiochemistry2005
Probing the affinity of SecA for signal peptide in different environments.
Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- The Structure ofInternational journal of molecular sciences · 2020Article
- 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
- 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
- Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Proteins · 2014Article
- Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome.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
- Characterization of the Escherichia coli SecA signal peptide-binding site.Journal of bacteriology · 2012Article
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Energetics of SecA dimerization.Journal of molecular biology · 2011Article
- Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2010Article
- Review
- Interactions that drive Sec-dependent bacterial protein transport.Biochemistry · 2007Review
- Selective photoaffinity labeling identifies the signal peptide binding domain on SecA.Journal of molecular biology · 2007Article
- Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.Biochimica et biophysica acta · 2007Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SecA, the peripheral subunit of the Escherichia coli preprotein translocase, interacts with a number of ligands during export, including signal peptides, membrane phospholipids, and nucleotides. Using fluorescence resonance energy transfer (FRET), we studied the interactions of wild-type (WT) and mutant SecAs with IAEDANS-labeled signal peptide, and how these interactions are modified in the presence of other transport ligands. We find that residues on the third alpha-helix in the preprotein cross-linking domain (PPXD) are important for the interaction of SecA and signal peptide. For SecA in aqueous solution, saturation binding data using FRET analysis fit a single-site binding model and yielded a Kd of 2.4 microM. FRET is inhibited for SecA in lipid vesicles relative to that in aqueous solution at a low signal peptide concentration. The sigmoidal nature of the binding curve suggests that SecA in lipids has two conformational states; our results do not support different oligomeric states of SecA. Using native gel electrophoresis, we establish signal peptide-induced SecA monomerization in both aqueous solution and lipid vesicles. Whereas the affinity of SecA for signal peptide in an aqueous environment is unaffected by temperature or the presence of nucleotides, in lipids the affinity decreases in the presence of ADP or AMP-PCP but increases at higher temperature. The latter finding is consistent with SecA existing in an elongated form while inserting the signal peptide into membranes.
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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.