ArticleBiochemistry2004
Demonstration of a specific Escherichia coli SecY-signal peptide interaction.
Article in Biochemistry, 2004. 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 abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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, 23 citations in OpenAlex.
- Site-saturation mutagenesis of mutant L-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase.Journal of industrial microbiology & biotechnology · 2017Article
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- Article
- Article
- Membrane protein insertion at the endoplasmic reticulum.Annual review of cell and developmental biology · 2011Review
- Transport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptide.Journal of bacteriology · 2010Article
- Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.Cell · 2007Article
- 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
- Molecular dynamics studies of the archaeal translocon.Biophysical journal · 2006Article
- Coarse grained protein-lipid model with application to lipoprotein particles.The journal of physical chemistry. B · 2006Article
- Probing the affinity of SecA for signal peptide in different environments.Biochemistry · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein translocation in Escherichia coli is initiated by the interaction of a preprotein with the membrane translocase composed of a motor protein, SecA ATPase, and a membrane-embedded channel, the SecYEG complex. The extent to which the signal peptide region of the preprotein plays a role in SecYEG interactions is unclear, in part because studies in this area typically employ the entire preprotein. Using a synthetic signal peptide harboring a photoaffinity label in its hydrophobic core, we examined this interaction with SecYEG in a detergent micellar environment. The signal peptide was found to specifically bind SecY in a saturable manner and at levels comparable to those that stimulate SecA ATPase activity. Chemical and proteolytic cleavage of cross-linked SecY and analysis of the signal peptide adducts indicate that the binding was primarily to regions of the protein containing transmembrane domains seven and two. The signal peptide-SecY interaction was affected by the presence of SecA and nucleotides in a manner consistent with the transfer of signal peptide to SecY upon nucleotide hydrolysis at SecA.
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What OpenQuestion holds
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.