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THE PLANT CELL, Vol 4, Issue 2 225-234, Copyright © 1992 by American Society of Plant Biologists

RESEARCH ARTICLES

A Maize Ribosome-Inactivating Protein Is Controlled by the Transcriptional Activator Opaque-2

H. W. Bass, C. Webster, G. R. OBrian, JKM. Roberts and R. S. Boston
Department of Botany, North Carolina State University, Raleigh, North Carolina 27695

Although synthesis of the cytosolic maize albumin b-32 had been shown to be controlled by the Opaque-2 regulatory locus, its function was unknown. We show here that b-32 is a member of the large and widely distributed class of toxic plant proteins with ribosome-inactivating activity. These ribosome-inactivating proteins (RIPs) are RNA N-glycosidases that remove a single base from a conserved 28S rRNA loop required for elongation factor 1[alpha] binding. Cell-free in vitro translation extracts were used to show that both maize and wheat ribosomes were resistant to molar excesses of b-32 but not to the dicotyledonous RIP gelonin. We extracted RIP activity from kernels during seed maturation and germination. The amount of RIP activity increased during germination, although the amount of b-32 protein remained fairly constant. Expression of a maize RIP gene under the control of an endosperm-specific transcriptional regulator may be an important clue prompting investigation of the biological basis for RIP expression in seeds of other plants.


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Copyright © 1992 by the American Society of Plant Biologists