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Gene Review

moaA  -  molybdopterin biosynthesis protein A

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0770, JW0764, bisA, chlA, narA
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Disease relevance of moaA


High impact information on moaA

  • The proteins encoded by the Escherichia coli genes moaA and moaC catalyse the first steps in MoCo synthesis [5].
  • However, relative to modA, binding of ModE to the moaA promoter appeared to be largely molybdate independent both in vitro and in vivo [6].
  • Footprint analysis of the moaA promoter revealed a single protected region located immediately upstream of the putative -35 consensus sequence and extending from position -202 to -174, relative to the start of translation [6].
  • N-terminal amino acid sequences for the moaA, B, C and E products confirmed the translational starts [7].
  • Genetic evidence is presented which strongly suggests that the molybdenum cofactor is a repressor of chlA expression [8].

Chemical compound and disease context of moaA


Biological context of moaA

  • Selection for growth on nitrate under anaerobic conditions yielded four plasmids which complemented mutants of the chlA, B, E and G types [11].
  • A clone containing a gene capable of complementing the chlA mutation SA493 was obtained on a large cosmid pJT1 [10].
  • However, the cofactor from the chlA strain mediated the dimerization of the nit-1 subunits in the presence and absence of molybdate to yield the 7.9S dimer [12].
  • Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes [13].
  • Through simultaneous selection for mutations in the two closely linked genes, gal and chlA, a variety of deletions of varying length, some extending through as much as 1 min of the chromosome, could be readily obtained [14].

Associations of moaA with chemical compounds

  • Heat-treated preparations from chlA and chlE mutants which do not possess molybdenum cofactor activity fail to restore the activation [15].
  • The partial purification of Protein PA has been achieved from various chlorate-resistant mutants (chlA-chlG) [9].
  • Conversely, well characterized mutants in any of chlA, B, D, E, G and N were also able to use citrate anaerobically [16].
  • The mixing of soluble fractions from chlA and chlB mutants grown under the appropriate conditions leads to the activation of nitrate reductase, formate benzyl-viologen oxidoreductase and trimethylamine-N-oxide reductase [17].

Other interactions of moaA


Analytical, diagnostic and therapeutic context of moaA


  1. Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis. Johnson, M.E., Rajagopalan, K.V. J. Bacteriol. (1987) [Pubmed]
  2. The narA locus of Synechococcus sp. strain PCC 7942 consists of a cluster of molybdopterin biosynthesis genes. Rubio, L.M., Flores, E., Herrero, A. J. Bacteriol. (1998) [Pubmed]
  3. Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis. Glaser, P., Danchin, A., Kunst, F., Zuber, P., Nakano, M.M. J. Bacteriol. (1995) [Pubmed]
  4. Stimulation of mutations suppressing the loss of replication control by small alcohols. Hayes, S., Hayes, C., Duncan, D., Bennett, V., Blushke, J. Mutat. Res. (1990) [Pubmed]
  5. Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency. Reiss, J., Cohen, N., Dorche, C., Mandel, H., Mendel, R.R., Stallmeyer, B., Zabot, M.T., Dierks, T. Nat. Genet. (1998) [Pubmed]
  6. Characterization of the ModE DNA-binding sites in the control regions of modABCD and moaABCDE of Escherichia coli. McNicholas, P.M., Rech, S.A., Gunsalus, R.P. Mol. Microbiol. (1997) [Pubmed]
  7. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Rivers, S.L., McNairn, E., Blasco, F., Giordano, G., Boxer, D.H. Mol. Microbiol. (1993) [Pubmed]
  8. Regulation of the chlA locus of Escherichia coli K12: involvement of molybdenum cofactor. Baker, K.P., Boxer, D.H. Mol. Microbiol. (1991) [Pubmed]
  9. Identification in various chlorate-resistant mutants of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K-12. Giordano, G., Saracino, L., Grillet, L. Biochim. Biophys. Acta (1985) [Pubmed]
  10. Reconstitution of plant nitrate reductase by Escherichia coli extracts and the molecular cloning of the chlA gene of Escherichia coli K12. Taylor, J.L., Bedbrook, J.R., Grant, F.J., Kleinhofs, A. J. Mol. Appl. Genet. (1983) [Pubmed]
  11. Cloning of seven differently complementing DNA fragments with chl functions from Escherichia coli K12. Reiss, J., Kleinhofs, A., Klingmüller, W. Mol. Gen. Genet. (1987) [Pubmed]
  12. Identification of the molybdenum cofactor in chlorate-resistant mutants of Escherichia coli. Amy, N.K. J. Bacteriol. (1981) [Pubmed]
  13. Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes. Pascal, M.C., Burini, J.F., Ratouchniak, J., Chippaux, M. Mol. Gen. Genet. (1982) [Pubmed]
  14. Positive selection of mutants with deletions of the gal-chl region of the Salmonella chromosome as a screening procedure for mutagens that cause deletions. Alper, M.D., Ames, B.N. J. Bacteriol. (1975) [Pubmed]
  15. Activation in vitro of respiratory nitrate reductase of Escherichia coli K12 grown in the presence of tungstate. Involvement of molybdenum cofactor. Saracino, L., Violet, M., Boxer, D.H., Giordano, G. Eur. J. Biochem. (1986) [Pubmed]
  16. Molybdenum cofactor negative mutants of Escherichia coli use citrate anaerobically. Clark, D.P. FEMS Microbiol. Lett. (1990) [Pubmed]
  17. A common pathway for the activation of several molybdoenzymes in Escherichia coli K12. Giordano, G., Violet, M., Medani, C.L., Pommier, J. Biochim. Biophys. Acta (1984) [Pubmed]
  18. Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1. Pitterle, D.M., Rajagopalan, K.V. J. Bacteriol. (1989) [Pubmed]
  19. Involvement of a low-molecular-weight substance in in vitro activation of the molybdoenzyme respiratory nitrate reductase from a chlB mutant of Escherichia coli. Boxer, D.H., Low, D.C., Pommier, J., Giordano, G. J. Bacteriol. (1987) [Pubmed]
  20. Precursor forms of the subunits of nitrate reductase in chlA and chlB mutants of Escherichia coli K12. Giordano, G., Grillet, L., Pommier, J., Terriere, C., Haddock, B.A., Azoulay, E. Eur. J. Biochem. (1980) [Pubmed]
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