Nucleic Acids Research, 1981, Vol. 9, No. 13 3105-3117
© 1981
ENZYMOLOGY |
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
+Institute of Biochemistry, Agricultural University Wolynska 35, 60-637 Poznan, Poland *Department of Chemistry, Imperial College of Science and Technology London SW7 2AY, UK
Received May 16, 1981. Evidence is presented that the editing mechanisms of aminoacyl-tRNA synthetases operate by two alternative pathways: pre-transfer, by hydrolysis of the non-cognate aminoacyl adenylate; post-transfer, by hydrolysis of the mischarged tRNA. The methionyl-tRNA synthetases from Escherichia coli and Bacillus stearothermophilus and isoleucyl-tRNA synthetase from E. coli, for example, are shown to reject misactivated homocysteine rapidly by the pretransfer route. A novel feature of this reaction is that homocysteine thiolactone is formed by the facile cyclisation of the homocysteinyl adenylate. Valyl-tRNA synthetases, on the other hand, reject the more readily activated non-cognate amino acids by primarily the post-transfer route. The features governing the choice of pathway are discussed.
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