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Mechanism and site of action of a ribosome‐inactivating protein type 1 from Dianthus barbatus which inactivates Escherichia coli ribosomes
Author(s) -
Prestle Jürgen,
Hornung Ellen,
Schönfelder Max,
Mundry Karl-Wolfgang
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80549-v
Subject(s) - ribosome , ribosome inactivating protein , ribosomal rna , biology , biochemistry , escherichia coli , protein biosynthesis , eukaryotic ribosome , a site , rna , microbiology and biotechnology , binding site , gene
A single chain ribosome‐inactivating protein with RNA N ‐glycosidase activity, here named Dianthin 29, was isolated from leaves of Dianthus barbatus L. Incubation of intact Escherichia coli ribosomes with Dianthin 29 and subsequent aniline treatment of the isolated rRNA releases a rRNA fragment of 243 nucleotides from 23 S rRNA. Nucleotide sequence studies showed that the site of N ‐glycosidic bond cleavage is at A‐2660 within the universally conserved sequence 5′‐AGUACG GAGGA‐3′ near the 3′‐end of 23/28 S rRNAs. To our knowledge, Dianthin 29 is the first ribosome‐inactivating protein which is shown to inactivate intact prokaryotic ribosomes in the same manner as eukaryotic ribosomes.