PARTIAL-PURIFICATION OF 2 PROTEINS WHICH SENSITIZE RIBOSOMES TO GELONIN - SENSITIZATION IS NOT LINKED TO PHOSPHORYLATION OF RIBOSOMAL-PROTEINS

Authors
BRIGOTTI M SPERTI S CARNICELLI D MONTANARO L
Citation
M. Brigotti et al., PARTIAL-PURIFICATION OF 2 PROTEINS WHICH SENSITIZE RIBOSOMES TO GELONIN - SENSITIZATION IS NOT LINKED TO PHOSPHORYLATION OF RIBOSOMAL-PROTEINS, Toxicon, 31(8), 1993, pp. 989-996
Citations number
22
Categorie Soggetti
Toxicology,"Pharmacology & Pharmacy
Journal title
Toxicon → ACNP
ISSN journal
00410101
Volume
31
Issue
8
Year of publication
1993
Pages
989 - 996
Database
ISI
SICI code
0041-0101(1993)31:8<989:PO2PWS>2.0.ZU;2-U
Abstract
Inactivation of ribosomes by gelonin, from Gelonium multiflorum, requi res ATP and extraribosomal protein(s) present in the rabbit reticulocy te lysate [SPERTI, S. et al. (1991) Biochem. J. 277, 281-284]. On the anion exchanger Mono Q the activity responsible for the sensitization of ribosomes to gelonin resolves in two peaks which both display a kin ase activity on ribosomal proteins. However, staurosporin, an inhibito r of several protein kinases, strongly inhibits phosphorylation of rib osomal proteins without affecting the gelonin-promoting activity of Mo no Q peaks. All the evidence collected contradicts a direct link betwe en sensitization to gelonin and phosphorylation of ribosomes.