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Nucleic Acids Research, 1980, Vol. 8, No. 9 2023-2037
© 1980

Articles

Two kinetically distinct tRNAile isoaccepton in Escherichia coli C6

Charles L. Harris and Farhad Marashi*

Department of Biochemistry, West Virginia University School of Medicine Morgantown, WV 26506, USA

Received March 25, 1980.

The isoleucine acceptance of tRNA from Escherichia coli C6 was previously shown to be influenced by the synthetase level (Marashi, F. and Harris, C.L. 1977. Biochim. Biophys. Acts 477, 84–88). We show here that the increased acceptance observed at higher enzyme levels is accompanied by an increase in the aminoacylation of one tRNAile species. Hence, tRNA2ile, a minor species at low enzyme levels, is a major isoacceptor after full aminoacylation. The two major isoleucine species have been purified using a combination of BD-cellulose, DEAE-Sephadex A-50 and methylated albumin kieselguhr chromatography. tRNA2ile (1511 pmoles lie/A260 of tRNA) was found to be slowly acylated, with a Vmax one-seventh that observed with tRNA3ile (1475 pmoles ile/A260). Two-dimensional TLC analysis of RNase T2 digests revealed differences in nucleotide content between the purified tRNAa. These results are discussed in terms of the presence of slow and fast tRNAile species in E. coli

*Current address: Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL


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