ArticleProceedings of the National Academy of Sciences of the United States of America2005
Dimeric SecA is essential for protein translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
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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
54 citing papers in PubMed, 102 citations in OpenAlex.
- Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Cellular dynamics of the SecA ATPase at the single molecule level.Scientific reports · 2021Article
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- The Structure ofInternational journal of molecular sciences · 2020Article
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis.Science advances · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.Protein science : a publication of the Protein Society · 2018Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- 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
- SecA functions in vivo as a discrete anti-parallel dimer to promote protein transport.Molecular microbiology · 2017Article
- Article
- Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.The Journal of biological chemistry · 2016Article
- Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Biochemistry · 2016Article
- Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Journal of bacteriology · 2015Article
- In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.PloS one · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities.Biochemical and biophysical research communications · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SecA facilitates bacterial protein translocation by its association with presecretory or membrane proteins and the SecYEG translocon channel. Once assembled, SecA ATPase undergoes cycles of membrane insertion and retraction at SecYEG that drive protein translocation in a stepwise fashion. SecA exists in equilibrium between a monomer and dimer, and association with its translocation ligands shifts this equilibrium dramatically. Here, we examined the proposal that protein translocation can occur by means of a SecA monomer. We produced a mutant SecA protein lacking residues 2-11, which was found to exist mostly as a monomer, and it was unable to complement a conditional-lethal secA mutant, was inactive for in vitro protein translocation, and was poorly active for translocation ATPase activity. Furthermore, we developed a technique termed membrane trapping, where wild-type SecA subunits became trapped within the membrane by overproduction of membrane-stuck mutant SecA proteins, and, in one case, a membrane-associated SecA heterodimer was demonstrated. Finally, we examined both endogenous and reconstituted membrane-bound SecA and found a significant level of SecA dimer in both cases, as assessed by chemical crosslinking. Collectively, our results strongly suggest that membrane-bound SecA dimer is critical for the protein translocation cycle, although these results cannot exclude participation of SecA monomer at some stage in the translocation process. Our findings have important implications regarding SecA motor function and translocon assembly and activation.
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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.