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Nucleic Acids Research, 1977, Vol. 4, No. 1 31-42
© 1977

Articles

Aminoacylation of tRNATrp from beef liver, yeast and E. coli by beef pancreas tryptopban-tRNA ligase. Stoichiometry of tRNATrp binding

Mireille Dorizzi*, Guy Merault**, Michel Fournier**, Julie Labouesse**, Gérard Keith***, Guy Dirheimer*** and Richard H. Buckingham****

Laboratoire de Biochimie BBC, Université de Bordeaux II Talence, France

**To whom reprint requests should be sent: Laboratoire de Biochimie BBC, Université de, Bordeaux II, 351, cours de la Libération 33405 Talence - France -

Received August 9, 1976.

The Michaelis constants and the maximum velocities in the aminoacyla-tion reaction of tRNATrp from beef liver, yeast and E. coli by pure beef pancreas tryptophan-tRNA ligase show that this mammalian enzyme recognizes and charges the two eucaryotic tRNAs with the same efficiency. The rate of aminoacylation of the procaryotic tRNATrP by the enzyme is three orders of magnitude lower. The pH optimum of aminoacylation is 8 for both eucaryotic tRNAs. The optimum magnesium concentration is different. The rate is maximum when magnesium concentration is stoichiometric to ATP concentration for tRNATrP from beef liver and 10 mM above ATP concentration for tRNATrp from yeast. The number of binding sites on the enzyme for the two eucaryotic tRNAs has been measured by equilibrium filtration on Sephadex G-100 and found equal to two.

*Present address : Laboratoire de Biochimie du Développement Institut de Biologie Moléculaire 2, place Jussieu, 75221 Paris cedex 05 - France -

***Present address : Institut de Biologie Moléculaire et Cellulaire, du C.N.R.S., 15, rue Descartes, 67000 Strasbourg - France -

****Present address : Institut de Biologie Physicochimique, Rue Pierre et Marie Curie, 75005 Paris - France -


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