ArticleProceedings of the National Academy of Sciences of the United States of America2006
Secretion signal recognition by YscN, the Yersinia type III secretion ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.Nature communications · 2019Article
- Assembly, structure, function and regulation of type III secretion systems.Nature reviews. Microbiology · 2017Review
- Type III-Dependent Translocation of HrpB2 by a Nonpathogenic hpaABC Mutant of the Plant-Pathogenic Bacterium Xanthomonas campestris pv. vesicatoria.Applied and environmental microbiology · 2016Article
- The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing.The Journal of biological chemistry · 2016Article
- YscU/FlhB of Yersinia pseudotuberculosis Harbors a C-terminal Type III Secretion Signal.The Journal of biological chemistry · 2015Article
- Control of type III secretion activity and substrate specificity by the cytoplasmic regulator PcrG.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Identification of secreted bacterial proteins by noncanonical amino acid tagging.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A substrate-fusion protein is trapped inside the Type III Secretion System channel in Shigella flexneri.PLoS pathogens · 2014Article
- Poison domains block transit of translocated substrates via the Legionella pneumophila Icm/Dot system.Infection and immunity · 2013Article
- LcrV mutants that abolish Yersinia type III injectisome function.Journal of bacteriology · 2013Article
- A novel C-terminal region within the multicargo type III secretion chaperone CesT contributes to effector secretion.Journal of bacteriology · 2013Article
- Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013Review
- Structure and function of the Type III secretion system of Pseudomonas aeruginosa.Current protein & peptide science · 2012Review
- A translocator-specific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function.Molecular microbiology · 2012Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion.Journal of bacteriology · 2011Article
- A sorting platform determines the order of protein secretion in bacterial type III systems.Science (New York, N.Y.) · 2011Article
- YopK regulates the Yersinia pestis type III secretion system from within host cells.Molecular microbiology · 2011Article
- Analysis of the expression, secretion and translocation of the Salmonella enterica type III secretion system effector SteA.PloS one · 2011Article
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Authors and funding
3 authors.
Funding
Abstract
Yersinia type III machines secrete protein substrates across the bacterial envelope. Secretion signals of some substrates have been identified; however, the mechanisms whereby these signals interact with type III machines are not known. Here we show that fusion of YopR, an early secretion substrate, to the N terminus of dihydrofolate reductase (DHFR) or other tightly folded proteins generates impassable hybrids that cannot travel the type III pathway. YopR hybrids capture YscN, the ATPase that provides energy for type III transport reactions, in the bacterial cytoplasm. Eleven N-terminal residues function as the YopR secretion signal, which is required for both binding to YscN and blocking the type III pathway. When expressed during type III machine assembly, YopR-DHFR blocks all secretion. Delayed expression of YopR-DHFR, when yersiniae have already engaged the type III pathway, blocks secretion of early (YscP) but not of late (effector Yops) substrates. These observations support a model whereby type III machines are programmed to secrete a sequence of proteins that can be disrupted when an impassable early substrate interacts with the YscN ATPase and blocks the transport of late substrates.
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