UNSPECIFIED (1991) SINGLE-CHAIN RIBOSOME INACTIVATING PROTEINS FROM PLANTS DEPURINATE ESCHERICHIA-COLI 23S RIBOSOMAL-RNA. FEBS LETTERS, 290 (1-2). pp. 65-68. ISSN 0014-5793

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Abstract

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
ISSN:	0014-5793
Date:	23 September 1991
Volume:	290
Number:	1-2
Number of Pages:	4
Page Range:	pp. 65-68
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/22445

Data sourced from Thomson Reuters' Web of Knowledge

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