Cytokinin activity of zeatin allylic phosphate, a natural compound

Abstract

Zeatin allylic phosphate (ZAP) retarded chlorophyll loss in the barleyleaf senescence assay at a concentration 20 times higher than for6-benzyladenine (BA): the effective concentrations for ZAP and BA were 10 and 0.5 , respectively. Sodium molybdate,an inhibitor of phosphatases, decreased the ZAP effective concentration to 0.5 without affecting leaf senescence andtrans-zeatin activity in the control. This demonstrates theimportance of the phosphate group for ZAP activity or its penetration into leafcells. ZAP up-regulated the protein kinase activity of the barley leaf chromatinwith concentration dependence similar to that oftrans-zeatin. Conversely, ZAP was 1000 times less activethan trans-zeatin in the competition with anti-idiotypeantibodies (raised against antibody to zeatin) for binding with atrans-zeatin-binding site oftrans-zeatin-binding protein ZBP67 isolated from barleyleaves. In contrast to trans-zeatin, ZAP did not activateRNA synthesis in the presence of ZBP in the in vitro systemcontaining chromatin and RNA polymerase I isolated from barley leaves. Insummary, data presented show that ZAP possesses cytokinin activity asdemonstrated by the retardation of barley leaf senescence, but moleculartarget(s) for ZAP in barley leaf cells differs, at least partially, from thesefor trans-zeatin. It seems possible that the cytokininactivity of ZAP results from its hydrolysis while producing zeatin.