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Gene Review

metJ  -  transcriptional repressor protein MetJ

Escherichia coli UTI89

 
 
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Disease relevance of metJ

 

High impact information on metJ

  • Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene [6].
  • We used three transcriptional repressor systems that are not part of any natural biological clock to build an oscillating network, termed the repressilator, in Escherichia coli [7].
  • Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS [8].
  • The 5' noncoding region was found to contain a "Met box" homologous to sequences suggestive of operator structures upstream from other methionine genes that are controlled by the product of the pleiotropic regulatory metJ gene [9].
  • The replication initiator protein of plasmid pSC101 is a transcriptional repressor of its own cistron [10].
 

Chemical compound and disease context of metJ

  • Mlc from Escherichia coli is a transcriptional repressor controlling the expression of a number of genes encoding enzymes of the phosphotransferase system (PTS), including ptsG and manXYZ, the specific enzyme II for glucose and mannose PTS transporters [11].
  • In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization (put) genes and thus is trifunctional [12].
  • The Escherichia coli repressor of biotin biosynthesis (BirA) is a unique transcriptional repressor which catalyzes synthesis of its own corepressor and catalyzes attachment of a cofactor to an essential metabolic enzyme [13].
  • Highly significant similarities were detected between the N-terminal region of P30 and those of GENA [the product of another unidentified gene (geneA) located upstream of the aceEF-lpd operon], and GNTR (a putative transcriptional repressor of the gluconate operon of Bacillus subtilis) [14].
  • Proline utilization A (PutA) from Escherichia coli is a multifunctional flavoprotein that is both a transcriptional repressor of the proline utilization (put) genes and a membrane-associated enzyme which catalyzes the 4-electron oxidation of proline to glutamate [15].
 

Biological context of metJ

  • Maxicell labeling experiments show that the plasmids code for a small peptide (12 kilodaltons) only when they carry a functional copy of metJ [16].
  • Role of the metF and metJ genes on the vitamin B12 regulation of methionine gene expression: involvement of N5-methyltetrahydrofolic acid [17].
  • It was therefore considered that only one point mutation in the metJ gene occurred in the L-methionine-producing mutants [18].
  • Both operons are transcribed from two divergent promoters, P(X) and P(M), and are negatively regulated by the MalR transcriptional repressor [19].
  • The Kruppel-associated box (KRAB) domain is a 75-amino acid transcriptional repressor module commonly found in eukaryotic zinc finger proteins [20].
 

Associations of metJ with chemical compounds

  • The metJ protein binds to a DNA fragment containing the potential operator of the metF gene with an affinity which is 10 times greater in the presence of S-adenosylmethionine than in its absence [21].
  • The cadCA operon of plasmid pI258, which confers resistance to the soft metals Cd(II), Pb(II) and Zn(II), is regulated by CadC, a metal-responsive transcriptional repressor [22].
  • PerR functions as a manganese-dependent, transcriptional repressor of the identified regulon [23].
  • However, in cells growing in malonate, malonate decarboxylase was induced, indicating that MdcY is a transcriptional repressor and that malonate or a product resulting from malonate metabolism should be the intracellular inducer of the mdc operon [24].
  • In the repressing region, there were three tandem C(A/T)CTCCC sequences and also a putative binding site of Mig1p, a transcriptional repressor which mediates glucose repression of several other genes [25].
 

Analytical, diagnostic and therapeutic context of metJ

References

  1. Transcript analysis reveals an extended regulon and the importance of protein-protein co-operativity for the Escherichia coli methionine repressor. Marincs, F., Manfield, I.W., Stead, J.A., McDowall, K.J., Stockley, P.G. Biochem. J. (2006) [Pubmed]
  2. Autoregulation by tandem promoters of the Salmonella typhimurium LT2 metJ gene. Urbanowski, M.L., Stauffer, G.V. J. Bacteriol. (1986) [Pubmed]
  3. The ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum is an iron-responsive transcriptional repressor in vitro. Friedman, Y.E., O'Brian, M.R. J. Biol. Chem. (2004) [Pubmed]
  4. The complete nucleotide sequence of the Pasteurella multocida toxin gene and evidence for a transcriptional repressor, TxaR. Petersen, S.K. Mol. Microbiol. (1990) [Pubmed]
  5. Identification of the minimal replicon of plasmid pMEA300 of the methylotrophic actinomycete Amycolatopsis methanolica. Vrijbloed, J.W., Jelínková, M., Hessels, G.I., Dijkhuizen, L. Mol. Microbiol. (1995) [Pubmed]
  6. Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene. Aiba, H. Cell (1983) [Pubmed]
  7. A synthetic oscillatory network of transcriptional regulators. Elowitz, M.B., Leibler, S. Nature (2000) [Pubmed]
  8. Thermoregulation of Shigella and Escherichia coli EIEC pathogenicity. A temperature-dependent structural transition of DNA modulates accessibility of virF promoter to transcriptional repressor H-NS. Falconi, M., Colonna, B., Prosseda, G., Micheli, G., Gualerzi, C.O. EMBO J. (1998) [Pubmed]
  9. Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Belfaiza, J., Parsot, C., Martel, A., de la Tour, C.B., Margarita, D., Cohen, G.N., Saint-Girons, I. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  10. The replication initiator protein of plasmid pSC101 is a transcriptional repressor of its own cistron. Vocke, C., Bastia, D. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  11. The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli. Schiefner, A., Gerber, K., Seitz, S., Welte, W., Diederichs, K., Boos, W. J. Biol. Chem. (2005) [Pubmed]
  12. Characterization of a bifunctional PutA homologue from Bradyrhizobium japonicum and identification of an active site residue that modulates proline reduction of the flavin adenine dinucleotide cofactor. Krishnan, N., Becker, D.F. Biochemistry (2005) [Pubmed]
  13. Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. Xu, Y., Nenortas, E., Beckett, D. Biochemistry (1995) [Pubmed]
  14. Overexpression and site-directed mutagenesis of the succinyl-CoA synthetase of Escherichia coli and nucleotide sequence of a gene (g30) that is adjacent to the suc operon. Buck, D., Guest, J.R. Biochem. J. (1989) [Pubmed]
  15. Regulation of PutA-membrane associations by flavin adenine dinucleotide reduction. Zhang, W., Zhou, Y., Becker, D.F. Biochemistry (2004) [Pubmed]
  16. Cloning of the methionine regulatory gene, metJ, of Escherichia coli K12 and identification of its product. Smith, A.A., Greene, R.C. J. Biol. Chem. (1984) [Pubmed]
  17. Role of the metF and metJ genes on the vitamin B12 regulation of methionine gene expression: involvement of N5-methyltetrahydrofolic acid. Cai, X.Y., Jakubowski, H., Redfield, B., Zaleski, B., Brot, N., Weissbach, H. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  18. Mechanism of L-methionine overproduction by Escherichia coli: the replacement of Ser-54 by Asn in the MetJ protein causes the derepression of L-methionine biosynthetic enzymes. Nakamori, S., Kobayashi, S., Nishimura, T., Takagi, H. Appl. Microbiol. Biotechnol. (1999) [Pubmed]
  19. MalR-mediated regulation of the Streptococcus pneumoniae malMP operon at promoter PM. Influence of a proximal divergent promoter region and competition between MalR and RNA polymerase proteins. Nieto, C., Puyet, A., Espinosa, M. J. Biol. Chem. (2001) [Pubmed]
  20. Biochemical analysis of the Kruppel-associated box (KRAB) transcriptional repression domain. Peng, H., Begg, G.E., Harper, S.L., Friedman, J.R., Speicher, D.W., Rauscher, F.J. J. Biol. Chem. (2000) [Pubmed]
  21. Interactions of the Escherichia coli methionine repressor with the metF operator and with its corepressor, S-adenosylmethionine. Saint-Girons, I., Belfaiza, J., Guillou, Y., Perrin, D., Guiso, N., Bârzu, O., Cohen, G.N. J. Biol. Chem. (1986) [Pubmed]
  22. Both metal binding sites in the homodimer are required for metalloregulation by the CadC repressor. Sun, Y., Wong, M.D., Rosen, B.P. Mol. Microbiol. (2002) [Pubmed]
  23. PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Horsburgh, M.J., Clements, M.O., Crossley, H., Ingham, E., Foster, S.J. Infect. Immun. (2001) [Pubmed]
  24. The malonate decarboxylase operon of Acinetobacter calcoaceticus KCCM 40902 is regulated by malonate and the transcriptional repressor MdcY. Koo, J.H., Cho, I.H., Kim, Y.S. J. Bacteriol. (2000) [Pubmed]
  25. Analysis of carbon source-regulated gene expression by the upstream region of the Candida tropicalis malate synthase gene in Saccharomyces cerevisiae. Umemura, K., Atomi, H., Izuta, M., Kanai, T., Takeshita, S., Ueda, M., Tanaka, A. Biochim. Biophys. Acta (1997) [Pubmed]
  26. On the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operator. García-Castellanos, R., Mallorquí-Fernández, G., Marrero, A., Potempa, J., Coll, M., Gomis-Rüth, F.X. J. Biol. Chem. (2004) [Pubmed]
 
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