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Gene Review

yscC  -  hypothetical protein

Yersinia enterocolitica

 
 
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Disease relevance of yscC

  • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis [1].
  • Amino acid sequence comparison revealed that MxiD is homologous to the YscC protein of Yersinia enterocolitica and to the C-terminal region of the PulD protein of Klebsiella pneumoniae [2].
  • The HrpH protein possessed similarity with several outer membrane proteins that are known to be involved in protein or phage secretion, including the Klebsiella oxytoca PulD protein, the Yersinia enterocolitica YscC protein, and the pIV protein of filamentous coliphages [3].
  • Protein YscC has a putative signal sequence and shares significant homology with outer membrane proteins involved in the secretion of pullulanase by Klebsiella pneumoniae (PulD) or in the assembly of filamentous bacteriophages (gene IV product) [4].
  • Computer-generated alignment algorithms predict that a homology exists between TcpE and the Klebsiella pneumoniae pullulanase secretion proteins PulD and PulF, the Xanthomonas campestris extracellular enzyme secretion factor XpsF, the Bacillus subtilis DNA competence protein ComG-ORF2, and the Yersinia enterocolitica Yop secretion determinant YscC [5].
 

High impact information on yscC

  • The production of the YscC complex is regulated by temperature and is reduced in strains carrying mutations in the yscN-U operon or in the virG gene [6].
  • Some psp null mutants have a growth defect when YscC is produced and a severe virulence defect in animals [7].
  • Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica [8].
  • The resulting expression plasmids for YscC, pETBlue-2-YscC and pTYB11-YscC, were regulated by robust T7 promoters that were induced with isopropyl-beta-D-thiogalactopyranoside [9].
 

Analytical, diagnostic and therapeutic context of yscC

  • Electron microscopy revealed that purified YscC complexes form ring-shaped structures of approximately 20 nm with an apparent central pore [6].
  • The specific immune response generated in YscC-vaccinated mice was relative to the particular purified protein, YscC or YscC-His(6), which was used for vaccination as determined by Western blot analysis and ELISA [9].

References

  1. Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis. Plano, G.V., Straley, S.C. J. Bacteriol. (1995) [Pubmed]
  2. MxiD, an outer membrane protein necessary for the secretion of the Shigella flexneri lpa invasins. Allaoui, A., Sansonetti, P.J., Parsot, C. Mol. Microbiol. (1993) [Pubmed]
  3. The Pseudomonas syringae pv. syringae 61 hrpH product, an envelope protein required for elicitation of the hypersensitive response in plants. Huang, H.C., He, S.Y., Bauer, D.W., Collmer, A. J. Bacteriol. (1992) [Pubmed]
  4. Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica. Michiels, T., Vanooteghem, J.C., Lambert de Rouvroit, C., China, B., Gustin, A., Boudry, P., Cornelis, G.R. J. Bacteriol. (1991) [Pubmed]
  5. Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus: analogies to other virulence factor secretory systems. Kaufman, M.R., Shaw, C.E., Jones, I.D., Taylor, R.K. Gene (1993) [Pubmed]
  6. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Koster, M., Bitter, W., de Cock, H., Allaoui, A., Cornelis, G.R., Tommassen, J. Mol. Microbiol. (1997) [Pubmed]
  7. PspG, a new member of the Yersinia enterocolitica phage shock protein regulon. Green, R.C., Darwin, A.J. J. Bacteriol. (2004) [Pubmed]
  8. Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica. Burghout, P., Beckers, F., de Wit, E., van Boxtel, R., Cornelis, G.R., Tommassen, J., Koster, M. J. Bacteriol. (2004) [Pubmed]
  9. Yersinia pestis outer membrane type III secretion protein YscC: expression, purification, characterization, and induction of specific antiserum. Goodin, J.L., Raab, R.W., McKown, R.L., Coffman, G.L., Powell, B.S., Enama, J.T., Ligon, J.A., Andrews, G.P. Protein Expr. Purif. (2005) [Pubmed]
 
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