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Utilization of Selenocysteine by a Cysteinyl-tRNA Synthetase from Phaseolus aureus
Author(s) -
Alex Shrift,
Daniel E. Bechard,
Craig Harcup,
L. Fowden
Publication year - 1976
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.58.3.248
Subject(s) - selenocysteine , biochemistry , chemistry , enzyme , phaseolus , cysteine , dimer , sodium dodecyl sulfate , sephadex , transfer rna , gel electrophoresis , urea , chromatography , biology , gene , organic chemistry , rna , botany
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.

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