Abstract:
: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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Barbieri L,Valbonesi P,Bonora E,Gorini P,Bolognesi A,Stirpe Fdoi
10.1093/nar/25.3.518subject
Has Abstractpub_date
1997-02-01 00:00:00pages
518-22issue
3eissn
0305-1048issn
1362-4962pii
gka111journal_volume
25pub_type
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