ArticleJournal of molecular biology2008
SecA, the motor of the secretion machine, binds diverse partners on one interactive surface.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed.
- Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.Journal of bacteriology · 2020Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
- Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.Journal of bacteriology · 2019Article
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Article
- The basis of asymmetry in the SecA:SecB complex.Journal of molecular biology · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Selective transport by SecA2: an expanding family of customized motor proteins.Biochimica et biophysica acta · 2014Review
- Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- 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
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Energetics of SecA dimerization.Journal of molecular biology · 2011Article
- Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.The Journal of biological chemistry · 2011Article
- The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: a possible general feature.Cellular & molecular biology letters · 2011Article
- New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysis.International journal of molecular sciences · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
In all living cells, regulated passage across membranes of specific proteins occurs through a universally conserved secretory channel. In bacteria and chloroplasts, the energy for the mechanical work of moving polypeptides through that channel is provided by SecA, a regulated ATPase. Here, we use site-directed spin labeling and electron paramagnetic resonance spectroscopy to identify the interactive surface used by SecA for each of the diverse binding partners encountered during the dynamic cycle of export. Although the binding sites overlap, resolution at the level of aminoacyl side chains allows us to identify contacts that are unique to each partner. Patterns of constraint and mobilization of residues on that interactive surface suggest a conformational change that may underlie the coupling of ATP hydrolysis to precursor 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.