Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions.
The extent of direct stimulation by spermine of reactions catalysed by nuclear N1 and N2 protein kinases purified from liver and prostate depends critically on the nature of the protein substrate. The chemically inert Co(NH3)36+ ion exerts effects on protein kinase reactions similar to those of spermidine or spermine. This enhancement of the phosphorylation of various protein substrates by polyamines or Co(NH3)63+ by purified nuclear protein kinase preparations was studied in relation to effects of temperature, pH and other factors. The results provide further support for our hypothesis [Ahmed, Wilson, Goueli & Williams-Ashman (1978) Biochem. J. 176, 739-750] that the enhancement of certain protein kinase reactions by polycations relates primarily to their interaction with the protein substrate, yielding more favourable conformations for phosphorylation by the protein kinase, rather than a direct effect on its catalytic activity.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D003035:Cobalt / Q000494:pharmacology; D004790:Enzyme Induction / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D010766:Phosphorylation; D010774:Phosvitin / Q000378:metabolism; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013096:Spermine / Q000494:pharmacology*
D003035:Cobalt; D010774:Phosvitin; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers; D011494:Protein Kinases; D013096:Spermine; C030862:cobalt ammonium complex