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Nucleic Acids Research, Vol 25, Issue 3 518-522, Copyright © 1997 by Oxford University Press


ARTICLES

Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA and poly(A)

L Barbieri, P Valbonesi, E Bonora, P Gorini, A Bolognesi and F Stirpe
Dipartimento di Patologia sperimentale dell'Universita degli Studi di Bologna Via San Giacomo 14, I-40126 Bologna, Italy. barbieri@alma.unibo.it

Ribosome-inactivating proteins (RIP) are a family of plant enzymes for which a unique activity was determined: rRNAN-glycosidase at a specific universally conserved position, A4324in the case of rat ribosomes. Recently we have shown that the RIP from Saponaria officinalis have a much wider substrate specificity: they are actually polynucleotide:adenosine glycosidases. Here we extend studies on substrate specificity to most known RIP: 52 purified proteins, both type 1 (single-chain) and type 2 (two chain, an enzymatic chain and a lectin chain) were examined for adenine release on various substrates including RNAs from different sources, DNA, and poly(A). All RIP depurinated extensively DNA and some released adenine from all adenine- containing polynucleotides tested. From experimental evidence the entire class of plant proteins, up to now called ribosome-inactivating proteins, may be classified as polynucleotide:adenosine glycosidases. The newly identified substrates may be implicated in the biological role(s) of RIP.
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