ArticleFEBS letters2007
Cross-linked SecA dimers are not functional in protein translocation.
Article in FEBS letters, 2007. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed.
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Binding of SecA ATPase monomers and dimers to lipid vesicles.Biochimica et biophysica acta. Biomembranes · 2020Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- SecAAA trimer is fully functional as SecAA dimer in the membrane: existence of higher oligomers?Biochemical and biophysical research communications · 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 solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.Biochemistry · 2013Article
- Using a low denaturant model to explore the conformational features of translocation-active SecA.Biochemistry · 2012Article
- SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.The Journal of biological chemistry · 2011Article
- The Accessory SecA2 System of Mycobacteria Requires ATP Binding and the Canonical SecA1.The Journal of biological chemistry · 2009Article
- Reexamination of the role of the amino terminus of SecA in promoting its dimerization and functional state.Journal of bacteriology · 2008Article
- Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: dissociation into monomers is not essential for protein translocation in Escherichia coli.Journal of bacteriology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The ATPase SecA is involved in post-translational protein translocation through the SecY channel across the bacterial inner membrane. SecA is a dimer that can dissociate into monomers with translocation activity. Here, we have addressed whether dissociation of the SecA dimer is required for translocation. We show that a dimer in which the two subunits are cross-linked by disulfide bridges is inactive in protein translocation, translocation ATPase, and binding to a lipid bilayer. In contrast, upon reduction of the disulfide bridges, the resulting monomers regain these activities. These data support the notion that dissociation of SecA dimers into monomers occurs during protein translocation.
Indexed as
Identifiers
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.