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Specific Degradation of a Plant Leucyl Transfer Ribonucleic Acid by a Factor in the Homologous Synthetase Preparation ^1,2

^a Department of Agricultural Chemistry, Oregon State University, Corvallis, Oregon 97331

Partially purified aminoacyl synthetase preparations from pea roots (Pisum sativum L. var. Alaska) contain a heat-labile factor which can degrade leucyl-tRNA₆^leu to a new species. The singular electrophoretic and chromatographic mobilities, the isoprenoid nucleoside content, and the charging characteristics of the new species (designated leucyl-tRNA_L^leu), suggest that it is a fragment of tRNA₆^leu containing at least that portion of the original molecule extending from the 3' terminus to the anticodon. Conversion appears to be highly specific since neither bulk tRNA, the other leucine tRNA subspecies, nor tyrosine, phenylalanine, or tryptophan tRNAs are susceptible to degradation during incubation with the synthetase preparation.

¹ This work was supported in part by a grant from the Herman Frasch Foundation and was undertaken while D.F.B. was a trainee in the Center for Environmental Management supported by United States Public Health Service Grant PHS-00210.

² Technical Paper 3305 from the Oregon State University Agricultural Experiment Station.