ArticleBiochemistry2012
Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed.
- The pod components of the Shigella T3SS sorting platform accommodate multiple copies of Spa33 (SctQ).PLoS pathogens · 2026Article
- Advances in Decoding Bacterial N-Terminal Proteoforms: Technologies, Challenges, and Functional Insights.Microorganisms · 2026Review
- Article
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica.Nature microbiology · 2024Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Differential regulation ofFrontiers in cellular and infection microbiology · 2023Article
- Composition and Biophysical Properties of the Sorting Platform Pods in theFrontiers in cellular and infection microbiology · 2021Article
- The Contribution of the Predicted Sorting Platform Component HrcQ to Type III Secretion inFrontiers in microbiology · 2021Article
- Lost and Found: Re-searching and Re-scoring Proteomics Data Aids Genome Annotation and Improves Proteome Coverage.mSystems · 2020Article
- Multiple proteins arising from a single gene: The role of the Spa33 variants in Shigella T3SS regulation.MicrobiologyOpen · 2019Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- Role of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system.PLoS pathogens · 2019Article
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system inThe Journal of biological chemistry · 2018Article
- Genes within Genes in Bacterial Genomes.Microbiology spectrum · 2018Review
- Functional Analysis of a Putative Type III Secretion System in Stress Adaption byFrontiers in microbiology · 2018Article
- A dynamic and adaptive network of cytosolic interactions governs protein export by the T3SS injectisome.Nature communications · 2017Article
- Control of type III protein secretion using a minimal genetic system.Nature communications · 2017Article
- The Architecture of the Cytoplasmic Region of Type III Secretion Systems.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The bacterial flagellar C-ring is composed of two essential proteins, FliM and FliN. The smaller protein, FliN, is similar to the C-terminus of the larger protein, FliM, both being composed of SpoA domains. While bacterial type III secretion (T3S) systems encode many proteins in common with the flagellum, they mostly have a single protein in place of FliM and FliN. This protein resembles FliM at its N-terminus and is as large as FliM but is more like FliN at its C-terminal SpoA domain. We have discovered that a FliN-sized cognate indeed exists in the Yersinia T3S system to accompany the FliM-sized cognate. The FliN-sized cognate, YscQ-C, is the product of an internal translation initiation site within the locus encoding the FliM-sized cognate YscQ. Both intact YscQ and YscQ-C were found to be required for T3S, indicating that the internal translation initiation site, which is conserved in some but not all YscQ orthologs, is crucial for function. The crystal structure of YscQ-C revealed a SpoA domain that forms a highly intertwined, domain-swapped homodimer, similar to those observed in FliN and the YscQ ortholog HrcQ(B). A single YscQ-C homodimer associated reversibly with a single molecule of intact YscQ, indicating conformational differences between the SpoA domains of intact YscQ and YscQ-C. A "snap-back" mechanism suggested by the structure can account for this. The 1:2 YscQ-YscQ-C complex is a close mimic of the 1:4 FliM-FliN complex and the likely building block of the putative Yersinia T3S system C-ring.
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.