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Gene Review

mraZ  -  RsmH methytransferase inhibitor

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0082, JW0079, yabB
 
 
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Disease relevance of mraZ

  • Heterologous expression of orfB, orfC and hsp18 genes in Escherichia coli significantly enhanced the viability of the host strain under acidic conditions [1].
 

High impact information on mraZ

  • A third open reading frame, orfC, positioned downstream of csgA may affect some functional property of curli since an insertion in this putative gene abolishes the autoagglutinating ability typical of curliated cells without affecting the production of the fibre [2].
  • The gene, designated gmhX, is part of a polycistronic operon (ice-2) containing two other genes, nlaB and orfC. nlaB encodes a lysophosphatidic-acid acyltransferase and orfC is predicted to encode a N-acetyltransferase [3].
  • We have found that mraW and mraZ are active genes, coding for two proteins with relative molecular masses of 34 800 and 17 300, respectively [4].
  • The protein encoded by orfC shares homologies with multi-drug resistance systems [1].
 

Biological context of mraZ

References

  1. Improved acid tolerance of a recombinant strain of Escherichia coli expressing genes from the acidophilic bacterium Oenococcus oeni. Morel, F., Delmas, F., Jobin, M.P., Diviès, C., Guzzo, J. Lett. Appl. Microbiol. (2001) [Pubmed]
  2. Expression of two csg operons is required for production of fibronectin- and congo red-binding curli polymers in Escherichia coli K-12. Hammar, M., Arnqvist, A., Bian, Z., Olsén, A., Normark, S. Mol. Microbiol. (1995) [Pubmed]
  3. gmhX, a novel gene required for the incorporation of L-glycero-D-manno-heptose into lipooligosaccharide in Neisseria meningitidis. Shih, G.C., Kahler, C.M., Carlson, R.W., Rahman, M.M., Stephens, D.S. Microbiology (Reading, Engl.) (2001) [Pubmed]
  4. mraW, an essential gene at the dcw cluster of Escherichia coli codes for a cytoplasmic protein with methyltransferase activity. Carrión, M., Gómez, M.J., Merchante-Schubert, R., Dongarrá, S., Ayala, J.A. Biochimie (1999) [Pubmed]
 
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