SINGLE-CHAIN RIBOSOME INACTIVATING PROTEINS FROM PLANTS DEPURINATE ESCHERICHIA-COLI 23S RIBOSOMAL-RNA
UNSPECIFIED. (1991) SINGLE-CHAIN RIBOSOME INACTIVATING PROTEINS FROM PLANTS DEPURINATE ESCHERICHIA-COLI 23S RIBOSOMAL-RNA. FEBS LETTERS, 290 (1-2). pp. 65-68. ISSN 0014-5793Full text not available from this repository.
The rRNA N-glycosidase activities of the catalytically active A chains of the heterodimeric ribosome inactivating proteins (RIPs) ricin and abrin, the single-chain RIPs dianthin 30, dianthin 32, and the leaf and seed forms of pokeweed antiviral protein (PAP) were assayed on E. coli ribosomes. All of the single-chain RIPs were active on E. coli ribosomes as judged by the release of a 243 nucleotide fragment from the 3' end of 23S rRNA following aniline treatment of the RNA. In contrast, E. coli ribosomes were refractory to the A chains of ricin and abrin. The position of the modification of 23S rRNA by dianthin 32 was determined by primer extension and found to be A2660, which lies in a sequence that is highly conserved in all species.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||FEBS LETTERS|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||23 September 1991|
|Number of Pages:||4|
|Page Range:||pp. 65-68|
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