Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
- 1 February 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 257 (3) , 723-727
- https://doi.org/10.1042/bj2570723
Abstract
.alpha.-Sarcin from Aspergillus giganteus and the ribosome-inactivating proteins (RIPs) from higher plants inactivate the 60 S ribosomal subunit. The former is an RNAase, whereas RIPs are N-glycosidases. The site of cleavage of RNA and that of N-glycosidic depurinization are at one nucleotide distance in 28 S rRNA [Endo and Tsurugi (1987) J. Biol. chem. 262, 8128-8130]. The effect of .alpha.-sarcin and that of RIPs on the interaction of elongation factors with Artemia salina (brine shrimp) ribosomes have been investigated. .alpha.-Sarcin inhibits both the EF1 (elongation factor 1)-dependent binding of aminoacyl-tRNA and the GTP-dependent binding of EF2 (elongation factor 2) to ribosomes, whereas two of the RIPs tested, ricin from Ricinus communis (castor bean) and volkensin from Adenia volkensii (kilyambiti), inhibit only the latter reaction. EF2 protects ribosomes from inactivation by both .alpha.-sarcin is increased by pretreatment of ribosomes with ricin. A. salina ribosomes were highly resistant to the third RIP tested, namely gelonin from Gelonium multiflorum. All four proteins tested have, however, a comparable activity on the rabbit reticulocyte-lysate system.This publication has 38 references indexed in Scilit:
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