ArticleThe EMBO journal1997
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.
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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
115 citing papers in PubMed.
- Discovery of CD4+ T cell-recognized B. pertussis antigens that reduce airway colonization.JCI insight · 2026Article
- Machine learning reveals proteome-encoded growth determinants underlying metabolic versatility ofmSystems · 2026Article
- Population Ecology of Glacier Bacteria from the View of Gene Flow inMicroorganisms · 2026Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Article
- Whole Cell Luminescence-Based Screen for Inhibitors of the Bacterial Sec Machinery.Biochemistry · 2024Article
- YajC, a predicted membrane protein, promotesFEMS microbes · 2024Article
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- The insertase YidC chaperones the polytopic membrane protein MelB inserting and folding simultaneously from both termini.Structure (London, England : 1993) · 2023Article
- Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.The Biochemical journal · 2023Article
- Cracking outer membrane biogenesis.Biochimica et biophysica acta. Molecular cell research · 2023Article
- Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Nucleic acids research · 2021Article
- Pushing the Envelope: The Mysterious Journey Through the Bacterial Secretory Machinery, and Beyond.Frontiers in microbiology · 2021Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.eLife · 2020Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- Membrane proteomic analysis reveals overlapping and independent functions of Streptococcus mutans Ffh, YidC1, and YidC2.Molecular oral microbiology · 2019Article
- Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography.The protein journal · 2019Review
- The Conserved Role of YidC in Membrane Protein Biogenesis.Microbiology spectrum · 2019Article
- The Dynamic ATP-Driven Mechanism of Bacterial Protein Translocation and the Critical Role of Phospholipids.Frontiers in microbiology · 2019Review
55 more citing papers are in PubMed but not listed here.
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
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli preprotein translocase contains a membrane-embedded trimeric complex of SecY, SecE and SecG (SecYEG) and the peripheral SecA protein. SecYE is the conserved functional 'core' of the SecYEG complex. Although sufficient to provide sites for high-affinity binding and membrane insertion of SecA, and for its activation as a preprotein-dependent ATPase, SecYE has only very low capacity to support translocation. The proteins encoded by the secD operon--SecD, SecF and YajC--also form an integral membrane heterotrimeric complex (SecDFyajC). Physical and functional studies show that these two trimeric complexes are associated to form SecYEGDFyajC, the hexameric integral membrane domain of the preprotein translocase 'holoenzyme'. Either SecG or SecDFyajC can support the translocation activity of SecYE by facilitating the ATP-driven cycle of SecA membrane insertion and de-insertion at different stages of the translocation reaction. Our findings show that each of the prokaryote-specific subunits (SecA, SecG and SecDFyajC) function together to promote preprotein movement at the SecYE core of the translocase.
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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.