Nucleic Acids Research, Vol 25, Issue 3 518-522, Copyright © 1997 by Oxford University Press
L Barbieri, P Valbonesi, E Bonora, P Gorini, A Bolognesi and F Stirpe
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.
ARTICLES
Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA and poly(A)
Dipartimento di Patologia sperimentale dell'Universita degli Studi di Bologna Via San Giacomo 14, I-40126 Bologna, Italy. barbieri@alma.unibo.it
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