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

ahpC  -  alkyl hydroperoxide reductase subunit C

Mycobacterium tuberculosis H37Rv

 
 
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 ahpC

  • Molecular analysis of isoniazid-resistant Mycobacterium tuberculosis isolates from England and Wales reveals the phylogenetic significance of the ahpC -46A polymorphism [1].
  • Using a green fluorescence protein vector (gfp)-ahpC reporter construct we present data showing that repression of ahpC of virulent M. tuberculosis also occurred during growth inside macrophages, whereas derepression in BCG was again seen under identical conditions [2].
 

High impact information on ahpC

  • Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis [3].
  • One of the genes affected by oxyR lesions, ahpC (encoding an alkylhydroperoxide reductase) may determine the intrinsic sensitivity of mycobacteria to isoniazid [4].
  • The ahpC gene, which encodes a critical subunit of alkyl hydroperoxide reductase, is one of the targets usually controlled by oxyR in bacteria [5].
  • In a demonstration of the critical role of ahpC in sensitivity to INH, insertional inactivation of ahpC on the chromosome of Mycobacterium smegmatis, a species naturally insensitive to INH, dramatically increased its susceptibility to this compound [5].
  • We have also isolated DNA sequences homologous to oxyR and ahpC from M. tuberculosis and Mycobacterium avium [6].
 

Chemical compound and disease context of ahpC

  • In this work, M. tuberculosis H37Rv and Mycobacterium smegmatis mc(2)155 ahpC knockout mutants were tested for sensitivity to reactive nitrogen intermediates, in particular peroxynitrite, a highly reactive combinatorial product of reactive nitrogen and oxygen species, and sensitivity to bactericidal mechanisms in resting and activated macrophages [7].
 

Biological context of ahpC

  • An increase in minimal inhibitory concentration for isoniazid was observed upon transformation of M. tuberculosis H37Rv with cosmids carrying the oxyR-ahpC region of M. leprae [8].
  • These do not include the oxidative stress genes ahpC and sodA, or those for siderophore production [9].
  • M. marinum AhpC levels detected by immunoblotting, were increased upon treatment with H2O2, in keeping with the presence of a functional OxyR and its binding site within the promoter region of ahpC [10].
  • In 9/10 isolates, mutations in the ahpC promoter region were located in the 105 bp oxyR-ahpC intergenic region [11].
  • To initiate investigations of the regulation of oxidative stress in mycobacteria and consequences of the elimination of oxyR in M. tuberculosis, in this work we tested the hypothesis that mycobacterial OxyR acts as a DNA binding protein and analyzed its interactions with the oxyR and ahpC promoters [12].
 

Associations of ahpC with chemical compounds

  • Mutations in katG, ahpC, and inhA were associated with rifampin resistance, but only katG315 mutations were associated with ethambutol resistance [13].
  • DESIGN: M. bovis ATCC35723 was electroporated with linear fragments of deoxyribonucleic acid (DNA) containing an ahpC gene interrupted by a kanamycin resistance gene [14].
 

Analytical, diagnostic and therapeutic context of ahpC

References

  1. Molecular analysis of isoniazid-resistant Mycobacterium tuberculosis isolates from England and Wales reveals the phylogenetic significance of the ahpC -46A polymorphism. Baker, L.V., Brown, T.J., Maxwell, O., Gibson, A.L., Fang, Z., Yates, M.D., Drobniewski, F.A. Antimicrob. Agents Chemother. (2005) [Pubmed]
  2. Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Springer, B., Master, S., Sander, P., Zahrt, T., McFalone, M., Song, J., Papavinasasundaram, K.G., Colston, M.J., Boettger, E., Deretic, V. Infect. Immun. (2001) [Pubmed]
  3. Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Sherman, D.R., Mdluli, K., Hickey, M.J., Arain, T.M., Morris, S.L., Barry, C.E., Stover, C.K. Science (1996) [Pubmed]
  4. The extreme sensitivity of Mycobacterium tuberculosis to the front-line antituberculosis drug isoniazid. Deretic, V., Pagán-Ramos, E., Zhang, Y., Dhandayuthapani, S., Via, L.E. Nat. Biotechnol. (1996) [Pubmed]
  5. Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid. Zhang, Y., Dhandayuthapani, S., Deretic, V. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  6. Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria. Sherman, D.R., Sabo, P.J., Hickey, M.J., Arain, T.M., Mahairas, G.G., Yuan, Y., Barry, C.E., Stover, C.K. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  7. Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages. Master, S.S., Springer, B., Sander, P., Boettger, E.C., Deretic, V., Timmins, G.S. Microbiology (Reading, Engl.) (2002) [Pubmed]
  8. Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid. Deretic, V., Philipp, W., Dhandayuthapani, S., Mudd, M.H., Curcic, R., Garbe, T., Heym, B., Via, L.E., Cole, S.T. Mol. Microbiol. (1995) [Pubmed]
  9. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Pym, A.S., Domenech, P., Honoré, N., Song, J., Deretic, V., Cole, S.T. Mol. Microbiol. (2001) [Pubmed]
  10. Oxidative stress response and characterization of the oxyR-ahpC and furA-katG loci in Mycobacterium marinum. Pagán-Ramos, E., Song, J., McFalone, M., Mudd, M.H., Deretic, V. J. Bacteriol. (1998) [Pubmed]
  11. Genomic mutations in the katG, inhA and aphC genes are useful for the prediction of isoniazid resistance in Mycobacterium tuberculosis isolates from Kwazulu Natal, South Africa. Kiepiela, P., Bishop, K.S., Smith, A.N., Roux, L., York, D.F. Tuber. Lung Dis. (2000) [Pubmed]
  12. Interactions of OxyR with the promoter region of the oxyR and ahpC genes from Mycobacterium leprae and Mycobacterium tuberculosis. Dhandayuthapani, S., Mudd, M., Deretic, V. J. Bacteriol. (1997) [Pubmed]
  13. Population genetics study of isoniazid resistance mutations and evolution of multidrug-resistant Mycobacterium tuberculosis. Hazbón, M.H., Brimacombe, M., Bobadilla del Valle, M., Cavatore, M., Guerrero, M.I., Varma-Basil, M., Billman-Jacobe, H., Lavender, C., Fyfe, J., García-García, L., León, C.I., Bose, M., Chaves, F., Murray, M., Eisenach, K.D., Sifuentes-Osornio, J., Cave, M.D., Ponce de León, A., Alland, D. Antimicrob. Agents Chemother. (2006) [Pubmed]
  14. Production of avirulent Mycobacterium bovis strains by illegitimate recombination with deoxyribonucleic acid fragments containing an interrupted ahpC gene. Wilson, T., Wards, B.J., White, S.J., Skou, B., de Lisle, G.W., Collins, D.M. Tuber. Lung Dis. (1997) [Pubmed]
  15. Molecular analysis of isoniazid resistance in Mycobacterium tuberculosis isolates recovered from South Korea. Kim, S.Y., Park, Y.J., Kim, W.I., Lee, S.H., Ludgerus Chang, C., Kang, S.J., Kang, C.S. Diagn. Microbiol. Infect. Dis. (2003) [Pubmed]
 
WikiGenes - Universities