ArticleJournal of bacteriology2009
Autoproteolysis of YscU of Yersinia pseudotuberculosis is important for regulation of expression and secretion of Yop proteins.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2024Review
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- An Interaction between the Inner Rod Protein YscI and the Needle Protein YscF Is Required to Assemble the Needle Structure of theThe Journal of biological chemistry · 2017Article
- Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in theThe Journal of biological chemistry · 2017Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- YscU/FlhB of Yersinia pseudotuberculosis Harbors a C-terminal Type III Secretion Signal.The Journal of biological chemistry · 2015Article
- Article
- Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein.Biophysical journal · 2014Article
- Genetically engineered frameshifted YopN-TyeA chimeras influence type III secretion system function in Yersinia pseudotuberculosis.PloS one · 2013Article
- Regulation of the Yersinia type III secretion system: traffic control.Frontiers in cellular and infection microbiology · 2013Review
- Role of EscP (Orf16) in injectisome biogenesis and regulation of type III protein secretion in enteropathogenic Escherichia coli.Journal of bacteriology · 2012Article
- Needle length control and the secretion substrate specificity switch are only loosely coupled in the type III secretion apparatus of Shigella.Microbiology (Reading, England) · 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
- Autoproteolysis and intramolecular dissociation of Yersinia YscU precedes secretion of its C-terminal polypeptide YscU(CC).PloS one · 2012Article
- Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion.Journal of bacteriology · 2011Article
- Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes.The Journal of biological chemistry · 2011Article
- Role of EscU auto-cleavage in promoting type III effector translocation into host cells by enteropathogenic Escherichia coli.BMC microbiology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YscU of Yersinia can be autoproteolysed to generate a 10-kDa C-terminal polypeptide designated YscU(CC). Autoproteolysis occurs at the conserved N downward arrowPTH motif of YscU. The specific in-cis-generated point mutants N263A and P264A were found to be defective in proteolysis. Both mutants expressed and secreted Yop proteins (Yops) in calcium-containing medium (+Ca(2+) conditions) and calcium-depleted medium (-Ca(2+) conditions). The level of Yop and LcrV secretion by the N263A mutant was about 20% that of the wild-type strain, but there was no significant difference in the ratio of the different secreted Yops, including LcrV. The N263A mutant secreted LcrQ regardless of the calcium concentration in the medium, corroborating the observation that Yops were expressed and secreted in Ca(2+)-containing medium by the mutant. YscF, the type III secretion system (T3SS) needle protein, was secreted at elevated levels by the mutant compared to the wild type when bacteria were grown under +Ca(2+) conditions. YscF secretion was induced in the mutant, as well as in the wild type, when the bacteria were incubated under -Ca(2+) conditions, although the mutant secreted smaller amounts of YscF. The N263A mutant was cytotoxic for HeLa cells, demonstrating that the T3SS-mediated delivery of effectors was functional. We suggest that YscU blocks Yop release and that autoproteolysis is required to relieve this block.
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