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Nucleic Acids Research, 1978, Vol. 5, No. 2 599-613
© 1978

Articles

Mammalian tRNA sulfurtransferase: properties of the enzyme in rat liver

Charles L. Harris*

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

Received January 6, 1978.

Transfer RNA sulfurtransferase activity was detected in 105,000 x g supernatant preparations from rat liver and several other rat tissues. Sulfur is transferred from [35S] cysteine to tRNA in a reaction which also requires ATP, Mg2+ and supernatant protein. While [35S] ß -mercaptopyruvate appeared to be a substrate for this enzyme, the reaction product was sensitive to deacylation and the reaction was inhibited by [32S] cysteine. Of the various nucleic acids tested, only tRNAs were effective sulfur acceptors, with rat liver tRNA being the poorest substrate. The [35S] reaction product was sensitive to ribonuclease, cochromatographed with tRNA on methylated-albumin kieselguhr columns, and was converted to nucleotide material after alkaline hydrolysis. DEAE-cellulose chromatography of the neutralized [35S] nucleotide digest revealed a single thionucleotide peak. These studies demonstrate that tRNA sulfurtransferase is present in various rat tissues, and that the requirements of the liver enzyme are similar to those of bacterial enzymes.

*With the technical assistance of Kurt Marin


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