The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

xylE  -  xylE

Pseudomonas putida

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of xylE


High impact information on xylE

  • The special feature of the system is the method of detection: colonies of cells that express xylE become yellow within seconds after selection plates are sprayed with catechol, a colorless substrate that is converted by CatO2ase to the yellow product, 2-hydroxymuconic semialdehyde [1].
  • The complete nucleotide sequence of xylE is presented [1].
  • Although xylE is functionally expressed in E. coli, CatO2ase is not detected in B. subtilis unless a fragment of DNA capable of promoting gene expression is ligated into a cleavage site on pTG402 upstream from xylE [1].
  • Strong complementarity between the ribosome binding site and 16S rRNA suggests that xylE mRNA translation in B. subtilis may commence at the same site as that recognized by P. putida [1].
  • Purified XylE is oxygen-sensitive and unstable in vitro, particularly in the presence of substituted catechol substrates, but it is stabilized in vivo by another protein, XylT, encoded by the xylT gene located just upstream of xylE [5].

Chemical compound and disease context of xylE

  • Metapyrocatechase which catalyzes the oxygenative ring cleavage of catechol to form alpha-hydroxymuconic epsilon-semialdehyde is encoded by the xylE gene on the TOL plasmid of Pseudomonas putida mt-2 [6].
  • The activities of the wild-type and mutant trpBA promoters, as monitored by xylE expression, were assayed in P. putida PpG1 and in E. coli [7].
  • Catechol-2,3-dioxygenase (C23O) of Pseudomonas putida, encoded by the xylE gene, was found to be sensitive to hydrogen peroxide (H(2)O(2)) when used as a reporter in gene fusion constructs [8].
  • A promoterless copy of xylE was placed under the transcriptional control of galP1, a glucose-repressed and galactose-induced promoter from Streptomyces lividans, and its expression was examined in bacterial colonies on agar plates or in liquid cultures grown in the presence of glucose or galactose as the sole carbon source [3].
  • Restriction enzyme analysis with HaeIII indicated similar restriction patterns for the xylE gene fragment between toluene DNA-extract and a type strain, Pseudomonas putida ATCC 23973 [9].

Biological context of xylE


Anatomical context of xylE


Associations of xylE with chemical compounds

  • Colonies of cells which express the xylE gene turn yellow shortly after being exposed with a solution of catechol [13].
  • No activities of the TOL plasmid encoded toluate dioxygenase and catechol 2,3-dioxygenase were detectable in strain CG220 [14].
  • By using a P. putida F1 todE mutant carrying this fusion on a plasmid, three cis-acting mutations that increased xylE expression enough to allow the todE strain to grow on toluene were isolated [7].
  • The level of xylE transcript from the trpBA promoter was increased in all three mutants [7].
  • Hydrogen peroxide sensitivity of catechol-2,3-dioxygenase: a cautionary note on use of xylE reporter fusions under aerobic conditions [8].

Other interactions of xylE


Analytical, diagnostic and therapeutic context of xylE


  1. Chromogenic identification of genetic regulatory signals in Bacillus subtilis based on expression of a cloned Pseudomonas gene. Zukowski, M.M., Gaffney, D.F., Speck, D., Kauffmann, M., Findeli, A., Wisecup, A., Lecocq, J.P. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  2. Cloning and sequence analysis of a catechol 2,3-dioxygenase gene from the nitrobenzene-degrading strain Comamonas sp JS765. Parales, R.E., Ontl, T.A., Gibson, D.T. J. Ind. Microbiol. Biotechnol. (1997) [Pubmed]
  3. xylE functions as an efficient reporter gene in Streptomyces spp.: use for the study of galP1, a catabolite-controlled promoter. Ingram, C., Brawner, M., Youngman, P., Westpheling, J. J. Bacteriol. (1989) [Pubmed]
  4. Cloning cassettes containing the reporter gene xylE. Clark, E., Cirvilleri, G. Gene (1994) [Pubmed]
  5. A novel -2Fe-2S- ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3-dioxygenase. Hugo, N., Armengaud, J., Gaillard, J., Timmis, K.N., Jouanneau, Y. J. Biol. Chem. (1998) [Pubmed]
  6. Complete nucleotide sequence of the metapyrocatechase gene on the TOI plasmid of Pseudomonas putida mt-2. Nakai, C., Kagamiyama, H., Nozaki, M., Nakazawa, T., Inouye, S., Ebina, Y., Nakazawa, A. J. Biol. Chem. (1983) [Pubmed]
  7. Up-promoter mutations in the trpBA operon of Pseudomonas aeruginosa. Han, C.Y., Crawford, I.P., Harwood, C.S. J. Bacteriol. (1991) [Pubmed]
  8. Hydrogen peroxide sensitivity of catechol-2,3-dioxygenase: a cautionary note on use of xylE reporter fusions under aerobic conditions. Hassett, D.J., Ochsner, U.A., Groce, S.L., Parvatiyar, K., Ma, J.F., Lipscomb, J.D. Appl. Environ. Microbiol. (2000) [Pubmed]
  9. Detection of catabolic genes in indigenous microbial consortia isolated from a diesel-contaminated soil. Milcic-Terzic, J., Lopez-Vidal, Y., Vrvic, M.M., Saval, S. Bioresour. Technol. (2001) [Pubmed]
  10. Plasmid-encoded regulation of colicin E1 gene expression. Ebina, Y., Takahara, Y., Shirabe, K., Yamada, M., Nakazawa, T., Nakazawa, A. J. Bacteriol. (1983) [Pubmed]
  11. Cloning and nucleotide sequence analysis of xylE gene responsible for meta-cleavage of 4-chlorocatechol from Pseudomonas sp. S-47. Noh, S.J., Kim, Y., Min, K.H., Karegoudar, T.B., Kim, C.K. Mol. Cells (2000) [Pubmed]
  12. Effect of temperature on the stability of plasmid pTG201 and productivity of xylE gene product in recombinant Escherichia coli: development of a two-stage chemostat with free and immobilized cells. Sayadi, S., Nasri, M., Berry, F., Barbotin, J.N., Thomas, D. J. Gen. Microbiol. (1987) [Pubmed]
  13. Construction of tracer plasmids for Bacillus sphaericus 1593 utilizing the xylE gene from Pseudomonas putida. Taylor, L.D., Burke, W.F. J. Invertebr. Pathol. (1991) [Pubmed]
  14. Loss of the TOL meta-cleavage pathway functions of Pseudomonas putida strain PaW1 (pWW0) during growth on toluene. Brinkmann, U., Ramos, J.L., Reineke, W. J. Basic Microbiol. (1994) [Pubmed]
  15. Construction of chimeric catechol 2,3-dioxygenase exhibiting improved activity against the suicide inhibitor 4-methylcatechol. Okuta, A., Ohnishi, K., Harayama, S. Appl. Environ. Microbiol. (2004) [Pubmed]
  16. Characterization of Pseudomonas putida mutants unable to catabolize benzoate: cloning and characterization of Pseudomonas genes involved in benzoate catabolism and isolation of a chromosomal DNA fragment able to substitute for xylS in activation of the TOL lower-pathway promoter. Jeffrey, W.H., Cuskey, S.M., Chapman, P.J., Resnick, S., Olsen, R.H. J. Bacteriol. (1992) [Pubmed]
  17. Molecular cloning of the xylL-xylE region from the P. putida TOL plasmid, pDK1. Voss, J.A., Khedairy, H., Baker, R.F., Benjamin, R.C. SAAS Bull. Biochem. Biotechnol. (1990) [Pubmed]
  18. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. Harayama, S., Rekik, M. J. Biol. Chem. (1989) [Pubmed]
  19. Relative expression and stability of a chromosomally integrated and plasmid-borne marker gene fusion in environmentally competent bacteria. Abebe, H.M., Seidler, R.J., Lindow, S.E., Short, K.A., Clark, E., King, R.J. Curr. Microbiol. (1997) [Pubmed]
  20. Flow cytometric detection of specific genes in genetically modified bacteria using in situ polymerase chain reaction. Porter, J., Pickup, R., Edwards, C. FEMS Microbiol. Lett. (1995) [Pubmed]
WikiGenes - Universities