Partial purification of two proteins which sensitize ribosomes to gelonin: sensitization is not linked to phosphorylation of ribosomal proteins.
Inactivation of ribosomes by gelonin, from Gelonium multiflorum, requires ATP and extraribosomal protein(s) present in the rabbit reticulocyte 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 kinase activity on ribosomal proteins. However, staurosporin, an inhibitor of several protein kinases, strongly inhibits phosphorylation of ribosomal proteins without affecting the gelonin-promoting activity of Mono Q peaks. All the evidence collected contradicts a direct link between sensitization to gelonin and phosphorylation of ribosomes.
Brigotti
M
M
Dipartimento di Patologia sperimentale, Università di Bologna, Italy.
Sperti
S
S
Carnicelli
D
D
Montanaro
L
L
D000818:Animals; D047388:Casein Kinases; D033364:Decapoda; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D011500:Protein Synthesis Inhibitors / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D012269:Ribosomal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000201:enzymology / Q000378:metabolism*
D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D012269:Ribosomal Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C025674:GEL protein, Gelonium multiflorum; D011494:Protein Kinases; D047388:Casein Kinases