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Plant Physiology 54:95-99 (1974)
© 1974 American Society of Plant Biologists

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Articles

Protein Kinase Activity Associated with Isolated Ribosomes from Peas and Lemna1

Robert A. B. Keates2 and Anthony J. Trewavas3

a Michigan State University-Atomic Energy Commission Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48823

Protein kinase (ATP:protein phosphokinase) has been found associated with ribosomes prepared from 5-day-old etiolated pea shoots and sterile cultures of Lemna minor. The enzyme catalyzes the phosphorylation of ribosomal proteins in vitro and may be involved in the formation of phosphoproteins in the ribosomes in vivo. Protein kinase sediments with ribosomes during sucrose density gradient centrifugation through a buffer containing 0.02 M KCl. Seventy per cent of the enzymic activity dissociates from the ribosomes in 0.3 M KCl, but the remaining protein kinase remains firmly bound in 0.7 M KCl. Cyclic AMP does not modify the activity of these protein kinases in vitro. Benzyladenine inhibits the protein kinase, but only at high concentrations of this cytokinin.

2 Present address: Department of Biochemistry, McMaster University, Hamilton, Ontario L8S 4J9, Canada. To whom reprint requests should be addressed.

3 On leave from: Department of Botany, University of Edinburgh, Mayfield Road, Edinburgh 9, Scotland.

1 This work was supported by United States Atomic Energy Commission Contract AT(11-1)-1338.




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