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Gene Review:

metG - methionyl-tRNA synthetase

Escherichia coli UTI89

Link, A.J. et al., Zimny, J. et al.

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Disease relevance of metG

Screening of a saturation mutagenesis library of the E. coli methionyl-tRNA synthetase (MetRS) led to the discovery of three MetRS mutants capable of incorporating the long-chain amino acid azidonorleucine into recombinant proteins with modest efficiency [1].

High impact information on metG

Homocysteine (Hcy) editing by methionyl-tRNA synthetase results in the formation of Hcy-thiolactone and initiates a pathway that has been implicated in human disease [2].

References

Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Link, A.J., Vink, M.K., Agard, N.J., Prescher, J.A., Bertozzi, C.R., Tirrell, D.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
Protective mechanisms against homocysteine toxicity: the role of bleomycin hydrolase. Zimny, J., Sikora, M., Guranowski, A., Jakubowski, H. J. Biol. Chem. (2006) [Pubmed]

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