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Gene Review:

katG - catalase-peroxidase HPI, heme b-containing

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3934, JW3914

Lee, J.H. et al., Sekiguchi, J. et al., Maslow, J.N. et al., Hoerter, J.D. et al., Blanchard, J.S., et al.

Tkachenko, Nesterova, Pshenichnov, Belkin, Smulski, Vollmer, Van Dyk, LaRossa, Shiba, Tsutsumi, Yano, Ihara, Kameda, Tanaka, Takahashi, Munekata, Rao, Kornberg, Maslow, Irani, Lee, Eckstein, Inamine, Belisle, Hoerter, Arnold, Ward, Sauer, Johnson, Fleming, Eisenstark,

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Disease relevance of katG

These hypotheses were tested directly through study of Hpx- (katG katE ahpCF) mutants of Escherichia coli, which lack enzymes to scavenge hydrogen peroxide (H2O2) [1].
We now report that the hypersensitivity of Deltafur mutants to UVA irradiation is associated with reduced hydroperoxidase I (HPI) and hydroperoxidase II (HPII) activity, and is associated with a decrease in the transcription of katE and katG genes [2].
A total of six recombinant Escherichia coli strains with the promoters from three oxidative-stress responsive genes, i.e. the katG, sodA and pqi-5 genes, fused to either the lux genes from Vibrio fischeri or X. luminescens were characterized and their responses to different chemicals compared [3].
An isogenic rtfA mutant of M. avium serovar 2 strain TMC724 was derived using a novel allelic exchange mutagenesis system utilizing a multicopy plasmid that contained the katG gene of Mycobacterium bovis and the gene encoding green fluorescent protein (gfp) [4].

High impact information on katG

Resistance to isoniazid can be caused either by mutations in the katG-encoded catalase-peroxidase, the enzyme responsible for drug activation, or by the molecular target, the inhA-encoded long chain enoyl-ACP reductase [5].
As a consequence, resistance to H2O2 was greatly diminished, particularly in katG (catalase HPI) mutants, implying a major role for the other catalase, the stationary-phase KatE (HPII), which is rpoS dependent [6].
We present the sequence of 176 kilobases of the Escherichia coli K-12 genome, from katG at 89.2 to an open reading frame (ORF) of unknown function at 92.8 minutes on the genetic map [7].
Escherichia coli isolates expressing individually five of the eight katG mutations showed loss of catalase and INH oxidation activities, and isolates carrying any of the five pncA mutations showed no pyrazinamidase activity, indicating that these mutations are associated with INH and PZA resistance, respectively [8].
A plasmid containing a transcriptional fusion of the Escherichia coli katG promoter to a truncated Vibrio fischeri lux operon (luxCDABE) was constructed [9].

Chemical compound and disease context of katG

Putrescine up-regulated, in a concentration-dependent manner, the expression levels of the oxyR and katG genes of Escherichia coli cells exposed to hydrogen peroxide [10].

Biological context of katG

Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli [11].
For example, the katG::V. fischeri lux strain, DPD2511, gave no discernible response due to its low level expression while a fusion of the katG promoter with the X. luminescens lux operon was clearly responsive and capable of detecting hydrogen peroxide down to about 1 ppm [3].

References

Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Park, S., You, X., Imlay, J.A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
Reduced hydroperoxidase (HPI and HPII) activity in the Deltafur mutant contributes to increased sensitivity to UVA radiation in Escherichia coli. Hoerter, J.D., Arnold, A.A., Ward, C.S., Sauer, M., Johnson, S., Fleming, T., Eisenstark, A. J. Photochem. Photobiol. B, Biol. (2005) [Pubmed]
Enhancement of the multi-channel continuous monitoring system through the use of Xenorhabdus luminescens lux fusions. Lee, J.H., Mitchell, R.J., Gu, M.B. Biosensors & bioelectronics. (2004) [Pubmed]
Biosynthetic specificity of the rhamnosyltransferase gene of Mycobacterium avium serovar 2 as determined by allelic exchange mutagenesis. Maslow, J.N., Irani, V.R., Lee, S.H., Eckstein, T.M., Inamine, J.M., Belisle, J.T. Microbiology (Reading, Engl.) (2003) [Pubmed]
Molecular mechanisms of drug resistance in Mycobacterium tuberculosis. Blanchard, J.S. Annu. Rev. Biochem. (1996) [Pubmed]
Inorganic polyphosphate and the induction of rpoS expression. Shiba, T., Tsutsumi, K., Yano, H., Ihara, Y., Kameda, A., Tanaka, K., Takahashi, H., Munekata, M., Rao, N.N., Kornberg, A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Blattner, F.R., Burland, V., Plunkett, G., Sofia, H.J., Daniels, D.L. Nucleic Acids Res. (1993) [Pubmed]
Detection of Multidrug Resistance in Mycobacterium tuberculosis. Sekiguchi, J., Miyoshi-Akiyama, T., Augustynowicz-Kopec, E., Zwolska, Z., Kirikae, F., Toyota, E., Kobayashi, I., Morita, K., Kudo, K., Kato, S., Kuratsuji, T., Mori, T., Kirikae, T. J. Clin. Microbiol. (2007) [Pubmed]
Oxidative stress detection with Escherichia coli harboring a katG'::lux fusion. Belkin, S., Smulski, D.R., Vollmer, A.C., Van Dyk, T.K., LaRossa, R.A. Appl. Environ. Microbiol. (1996) [Pubmed]
The role of the natural polyamine putrescine in defense against oxidative stress in Escherichia coli. Tkachenko, A., Nesterova, L., Pshenichnov, M. Arch. Microbiol. (2001) [Pubmed]
Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli. Triggs-Raine, B.L., Doble, B.W., Mulvey, M.R., Sorby, P.A., Loewen, P.C. J. Bacteriol. (1988) [Pubmed]

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