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Gene Review

fmt  -  10-formyltetrahydrofolate:L-methionyl...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3274, JW3249, yhdD
 
 
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Disease relevance of fmt

  • A gene putatively encoding Met-tRNAi formyltransferase, fmt, was found downstream of the deformylase gene except in L. lactis, Mycoplasma genitalium, Calothrix PCC7601 and T. maritima [1].
  • Knockout experiments in Streptococcus pneumoniae R6x indicate that the transformylase (fmt) and deformylase (defB) genes are essential and that a def paralog (defA) is not [2].
  • The genetic organization near the recently cloned fmt gene, encoding Escherichia coli methionyl-tRNA(fMet) formyltransferase (J. M. Guillon, Y. Mechulam, J. M. Schmitter, S. Blanquet, and G. Fayat, J. Bacteriol. 174:4294-4301, 1992), has been studied [3].
 

High impact information on fmt

  • The def gene could be inactivated if the fmt gene was also inactivated, or if biosynthesis of N10-formyl-tetrahydrofolate, the formyl donor in methionyl-tRNA(i) transformylation, was blocked by trimethoprim [4].
  • It forms an operon with the fmt gene, that encodes the initiator methionyl-tRNA(i) transformylase, which was recently characterized (Guillon et al., J. Bacteriol., 174, 4294-4301, 1992) [4].
  • Actinonin-resistant mutants of S. pneumoniae ATCC 49619 harbor mutations in defB but not in fmt [2].
  • MTF from eubacteria contains an approximately 100-amino acid C-terminal extension that is not found in the E. coli glycinamide ribonucleotide formyltransferase, which, like MTF, use N(10)-formyltetrahydrofolate as a formyl group donor [5].
  • Peptidoglycan hydrolase, LytF (CwlE), was determined to be identical to YhdD (deduced cell wall binding protein) by zymography after insertional inactivation of the yhdD gene [6].
 

Biological context of fmt

  • Most of the wide deviations of amino acid usage observed in def- and fmt-encoded proteins among species is best accounted for by the nucleotide composition of genomes [1].
  • When the gene fusion technique was used for probing, no effect on fmt expression of the concentrations of methionyl-tRNA(fMet) formyltransferase or tRNA(fMet) could be found [3].
  • The possibility that the fmt gene, the product of which is present in excess to ensure full N acylation of methionyl-tRNA(fMet), could be expressed in a constitutive manner is discussed [3].
  • Moreover, the nucleotide sequence of a 1,379-bp fragment upstream from fmt reveals two additional open reading frames, in the opposite polarity [3].
  • The fmt gene, which starts at a GUG codon, is cotranscribed with another gene, fms, and the transcription start site of this operon has been precisely mapped [3].
 

Associations of fmt with chemical compounds

  • Susceptibility to actinonin was restored when the wild-type fmt gene was introduced into these mutant strains [7].
 

Analytical, diagnostic and therapeutic context of fmt

References

  1. A survey of polypeptide deformylase function throughout the eubacterial lineage. Mazel, D., Coïc, E., Blanchard, S., Saurin, W., Marlière, P. J. Mol. Biol. (1997) [Pubmed]
  2. Resistance of Streptococcus pneumoniae to deformylase inhibitors is due to mutations in defB. Margolis, P., Hackbarth, C., Lopez, S., Maniar, M., Wang, W., Yuan, Z., White, R., Trias, J. Antimicrob. Agents Chemother. (2001) [Pubmed]
  3. The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control. Meinnel, T., Guillon, J.M., Mechulam, Y., Blanquet, S. J. Bacteriol. (1993) [Pubmed]
  4. Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. Mazel, D., Pochet, S., Marlière, P. EMBO J. (1994) [Pubmed]
  5. Escherichia coli methionyl-tRNA formyltransferase: role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA. Gite, S., Li, Y., Ramesh, V., RajBhandary, U.L. Biochemistry (2000) [Pubmed]
  6. Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis. Ohnishi, R., Ishikawa, S., Sekiguchi, J. J. Bacteriol. (1999) [Pubmed]
  7. Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene. Margolis, P.S., Hackbarth, C.J., Young, D.C., Wang, W., Chen, D., Yuan, Z., White, R., Trias, J. Antimicrob. Agents Chemother. (2000) [Pubmed]
 
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