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Gene Review

yihX  -  alpha-D-glucose-1-phosphate phosphatase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of yihX

 

High impact information on yihX

 

Chemical compound and disease context of yihX

 

Biological context of yihX

  • CheZ is the phosphatase of CheY, the response regulator in bacterial chemotaxis [6].
  • Transcriptional and translational cat and phoA fusions to invA (the proximal gene in the invABC operon) were constructed, and their expression was studied by measuring the levels of alkaline phosphatase or chloramphenicol acetyltransferase activity in mutants grown under different conditions [14].
  • In contrast, the PhoP constitutively inactive phenotype observed for the PhoQ-T48L mutant resulted from both decreased autokinase activity and increased phosphatase activity [15].
  • It is concluded that the Salmonella SigD protein deprived of its phosphatase activity is able to disrupt yeast morphogenesis by interfering with Cdc42 function, opening the possibility that the SigD N-terminal region might directly modulate small GTPases from the host during infection [16].
  • Statistical analysis revealed significant differences between the horses which survived and those which died in their packed cell volumes, white blood cell counts, neutrophil counts, serum albumin concentrations and alkaline phosphatase activities [17].
 

Anatomical context of yihX

  • In reporter gene assays nidulal (1) preferentially activated the transcription factor complex AP-1-mediated expression of secreted alkaline phosphatase in COS-7 cells [18].
  • The identity of the epithelial cells (in the villus tip-to-crypt cell gradient) was monitored by measuring their intracellular alkaline phosphatase activity, while scanning electron microscopy was used to visualize the effects of infection and cell elution techniques [19].
  • The activities of brush border sucrase (72% P < 0.001) and lactase (47% P < 0.01) and alkaline phosphatase (43% P < 0.01) were also significantly reduced in infected animals as compared to the controls [20].
 

Associations of yihX with chemical compounds

 

Other interactions of yihX

  • A survey of Salmonella typhimurium enzymes possessing phosphatase or phosphodiesterase activity was made using several different growth conditions [25].
  • Acid phosphatase is regulated via carbon-starvation; although the C. freundii strains overexpressed phosphatase activity in carbon-limiting continuous culture, this was approximately 20-fold less than the activity of strain N14 grown similarly [2].
  • Metal uptake is mediated by the activity of a periplasmic acid-type phosphatase that liberates inorganic phosphate to provide the precipitant ligand for heavy metals presented to the cells [13].
 

Analytical, diagnostic and therapeutic context of yihX

  • First, after immunoprecipitation of MHC class I from NXS2 cells, peptides were eluted and examined in tandem-MS analysis which lead to the identification of three novel natural MHC class I peptide ligands, TEALPVKLI from ribonucleotide reductase M2, NEYIMSLI from Ser/Thr protein phosphatase 2A and FEMVSTLI with unknown origin [26].

References

  1. Elimination of host cell PtdIns(4,5)P(2) by bacterial SigD promotes membrane fission during invasion by Salmonella. Terebiznik, M.R., Vieira, O.V., Marcus, S.L., Slade, A., Yip, C.M., Trimble, W.S., Meyer, T., Finlay, B.B., Grinstein, S. Nat. Cell Biol. (2002) [Pubmed]
  2. Phosphatase production and activity in Citrobacter freundii and a naturally occurring, heavy-metal-accumulating Citrobacter sp. Montgomery, D.M., Dean, A.C., Wiffen, P., Macaskie, L.E. Microbiology (Reading, Engl.) (1995) [Pubmed]
  3. Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis. Madhusudan, n.u.l.l., Zapf, J., Whiteley, J.M., Hoch, J.A., Xuong, N.H., Varughese, K.I. Structure (1996) [Pubmed]
  4. Investigation of cytotoxic, genotoxic, mutagenic, and estrogenic effects of the flame retardants tris-(2-chloroethyl)-phosphate (TCEP) and tris-(2-chloropropyl)-phosphate (TCPP) in vitro. Föllmann, W., Wober, J. Toxicol. Lett. (2006) [Pubmed]
  5. The attenuated sopB mutant of Salmonella enterica serovar Typhimurium has the same tissue distribution and host chemokine response as the wild type in bovine Peyer's patches. Reis, B.P., Zhang, S., Tsolis, R.M., Bäumler, A.J., Adams, L.G., Santos, R.L. Vet. Microbiol. (2003) [Pubmed]
  6. Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis. Blat, Y., Eisenbach, M. J. Biol. Chem. (1996) [Pubmed]
  7. The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin. O'Toole, G.A., Trzebiatowski, J.R., Escalante-Semerena, J.C. J. Biol. Chem. (1994) [Pubmed]
  8. Late events in B cell activation. Expression of membrane alkaline phosphatase activity. Burg, D.L., Feldbush, T.L. J. Immunol. (1989) [Pubmed]
  9. The identification of distinct protein kinases and phosphatases in the prokaryote Salmonella typhimurium. Wang, J.Y., Koshland, D.E. J. Biol. Chem. (1981) [Pubmed]
  10. Regulation of phosphatase activity in bacterial chemotaxis. Blat, Y., Gillespie, B., Bren, A., Dahlquist, F.W., Eisenbach, M. J. Mol. Biol. (1998) [Pubmed]
  11. Modulation of chloride secretory responses and barrier function of intestinal epithelial cells by the Salmonella effector protein SigD. Bertelsen, L.S., Paesold, G., Marcus, S.L., Finlay, B.B., Eckmann, L., Barrett, K.E. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
  12. Bifunctionality and polarized infidelity at the hisB locus of Aspergillus nidulans. Millington Ward, A.M., Reuser, J.A., Scheele, J.Y., van Lohuizen, E.J., van Gorkum van Diepen, I.R., Klasen, E.A., Bresser, M. Mol. Gen. Genet. (1984) [Pubmed]
  13. Phosphatase-mediated heavy metal accumulation by a Citrobacter sp. and related enterobacteria. Macaskie, L.E., Bonthrone, K.M., Rouch, D.A. FEMS Microbiol. Lett. (1994) [Pubmed]
  14. Expression of Salmonella typhimurium genes required for invasion is regulated by changes in DNA supercoiling. Galán, J.E., Curtiss, R. Infect. Immun. (1990) [Pubmed]
  15. Mutational analysis of the residue at position 48 in the Salmonella enterica Serovar Typhimurium PhoQ sensor kinase. Sanowar, S., Martel, A., Moual, H.L. J. Bacteriol. (2003) [Pubmed]
  16. Inhibition of Cdc42-dependent signalling in Saccharomyces cerevisiae by phosphatase-dead SigD/SopB from Salmonella typhimurium. Rodr??guez-Escudero, I., Rotger, R., Cid, V.J., Molina, M. Microbiology (Reading, Engl.) (2006) [Pubmed]
  17. Diarrhoea in adult horses: a survey of clinical cases and an assessment of some prognostic indices. Mair, T.S., de Westerlaken, L.V., Cripps, P.J., Love, S. Vet. Rec. (1990) [Pubmed]
  18. Nidulal, a novel inducer of differentiation of human promyelocytic leukemia cells from Nidula candida. Erkel, G., Becker, U., Anke, T., Sterner, O. J. Antibiot. (1996) [Pubmed]
  19. Elevated cAMP in intestinal epithelial cells during experimental cholera and salmonellosis. Peterson, J.W., Molina, N.C., Houston, C.W., Fader, R.C. Toxicon (1983) [Pubmed]
  20. Effect of Salmonella typhimurium toxin on the expression of rabbit intestinal functions. Chitra, n.u.l.l., Sun, P., Mahmood, S. Indian J. Med. Res. (2002) [Pubmed]
  21. 3-Substituted indolizine-1-carbonitrile derivatives as phosphatase inhibitors. Weide, T., Arve, L., Prinz, H., Waldmann, H., Kessler, H. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
  22. Protein engineering of class-A non-specific acid phosphatase (PhoN) of Salmonella typhimurium: Modulation of the pH-activity profile. Makde, R.D., Dikshit, K., Kumar, V. Biomol. Eng. (2006) [Pubmed]
  23. Hematologic and serum biochemical changes in Salmonella ser Typhimurium-infected calves. Santos, R.L., Tsolis, R.M., Bäumler, A.J., Adams, L.G. Am. J. Vet. Res. (2002) [Pubmed]
  24. Biochemical changes in fowl serum during infection with Salmonella typhimurium. Itoh, N., Kikuchi, N., Hiramune, T. J. Vet. Med. Sci. (1996) [Pubmed]
  25. Resolution and purification of three periplasmic phosphatases of Salmonella typhimurium. Kier, L.D., Weppelman, R., Ames, B.N. J. Bacteriol. (1977) [Pubmed]
  26. Vaccination with minigenes encoding for novel 'self' antigens are effective in DNA-vaccination against neuroblastoma. Huebener, N., Lange, B., Lemmel, C., Rammensee, H.G., Strandsby, A., Wenkel, J., Jikai, J., Zeng, Y., Gaedicke, G., Lode, H.N. Cancer Lett. (2003) [Pubmed]
 
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