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JBC, Vol. 254, Issue 19, 9429-9440, Oct, 1979
J. T. Fayerman, M. C. Vann, L. S. Williams and H. E. Umbarger
A mutation in the ilvU locus of Escherichia coli has led to a complex
phenotype that included resistance to thiaisoleucine, a loss of
derepressibility of isoleucyl tRNA synthetase, and an alteration of the
RPC-5 chromatographic profile of the branched-chain aminoacyl-tRNA's. The
alterations were manifest in an increase in the amount of Species 2 of both
tRNAIle and tRNAVal at the expense of Species 1. A similar alteration, but
independent of (and additive to) that caused by the ilvU mutation, was
observed upon limitation of either isoleucine or valine. The shift in
profile caused by limitation was also independent of the reduced growth
rate or the derepression of the isoleucine and valine biosynthetic enzymes
that also result from limitation. During chloramphenicol treatment nearly
all tRNAIle and tRNAVal formed appears as species 2. Upon recovery from
chloramphenicol, Species 2 of both acceptors are converted to Species 1. It
is proposed that the ilvU product not only allows derepression of
isoleucyl-tRNA synthetase but also retards the conversion of tRNA2Ile to
tRNA1Ile and that of tRNA2Val to tRNA1Val. The mutated ilvU loci abolish
the derepression and are more efficient in retarding the conversion.
ilvU, a locus in Escherichia coli affecting the derepression of isoleucyl-tRNA synthetase and the RPC-5 chromatographic profiles of tRNAIle and tRNAVal
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