Specific interaction of cytokinin binding protein with 40S ribosomal subunits in the presence of cytokinin in vitro

概要

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Cytokinin binding protein (CB-protein) prepared from tobacco (Nicotiana tabacum var. Bright Yellow) leaves by affinity chromatography was found to bind specifically to 40S ribosomal subunits but not to 60S subunits in vitro at 37℃. The binding capacity to 0.5 M KCl-washed ribosomes was about 10 times higher than that to un-washed ribosomes, stimulated 3 times by a synthetic cytokinin, benzyladenine, and was completely inhibited by 0.4 M KCl. Under optimum conditions, 2 to 3 moles of CB-protein bound to one KCl-washed ribosomal subunit. About 80-70, 10-8, 8-4, 6 and 3% of total CB-protein were present in Supernatant, ribosomal, mitochondrial, chloroplast and nuclear fractions, respectively. A considerable amount of CB-protein was isolated from KCl-wash of ribosomes which is believed to contain the initiation factors for protein synthesis. The roles of CB-protein in protein synthesis are discussed.
日本植物生理学会の論文