Mechanism and site of action of a ribosome-inactivating protein type 1 from Dianthus barbatus which inactivates Escherichia coli ribosomes.

Abstract:

: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'-AGUACGAGAGGA-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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Prestle J,Hornung E,Schönfelder M,Mundry KW

doi

10.1016/0014-5793(92)80549-v

keywords:

subject

Has Abstract

pub_date

1992-02-10 00:00:00

pages

250-2

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80549-V

journal_volume

297

pub_type

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