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Plant Physiology 58:248-252 (1976)
© 1976 American Society of Plant Biologists

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Articles

Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus1

Alex Shrifta, Daniel Becharda,2 and Craig Harcupa,3

Leslie Fowdenb

a Department of Biological Sciences, State University of New York, Binghamton, New York 13901, Rothamsted Experimental Station, Harpenden, Herts. AL5 2JQ England

An L-cysteinyl-tRNA synthetase (EC 6.1.1.16) from Phaseolus aureus has been purified approximately 200-fold. The enzyme uses selenocysteine as substrate in the ATP-PPi exchange assay; other cysteine analogs were inactive. The molecular weight as determined by Sephadex G-200 column chromatography is about 61,000; sodium dodecyl sulfate and 8 M urea acrylamide gel electrophoresis indicate that the enzyme is a dimer consisting of two identical monomers of molecular weight 30,000. A method for the preparation of selenocysteine from selenocystine is described.

2 Present address: State University of New York Medical Center, Syracuse, New York 13210.

3 Present address: Georgetown University School of Medicine, Washington, D. C. 20007.

1 This research was carried out in part at University College, London, Department of Botany and Microbiology, under tenure of Senior Research Fellowship GM53476 to A. S. from the United States Public Health Service, and in part under United States Public Health Service Grant ES00807.




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