Dual specificity of casein kinase II from the yeast Yarrowia lipolytica.
In the case of protein kinases, and especially in the case of casein kinase II (CKII), a link has been found between the type of the amino acids autophosphorylated and the targeted amino acids on the substrates. In the presence of Mg2+, CKII from the yeast Yarrowia lipolytica is autophosphorylated on serines and threonines, and a serine threonine kinase activity is found predominantly when casein is used as substrate. In the presence of Mn2+, CKII autophosphorylation is inhibited on serines, and autophosphorylation on tyrosines, negligible in the former case, becomes significant. Tyrosine phosphorylation is then found to occur on casein. Mn2+ transforms CKII into a protein kinase with dual specificity, shifting its specificity from serine/threonine kinase towards a serine/threonine and tyrosine kinase. Mn2+ decreases the level of serine and threonine phosphorylation observed, while on the other hand promoting tyrosine kinase activity.
Laboratoire de chimie biologique, INRA/INA/PG, Centre de biotechnologie agro-industrielle, Thiverval-Grignon, France.
T
T
Chardot
H
H
Shen
J C
JC
Meunier
D047390:Casein Kinase II; D002413:Cations, Divalent; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism* / Q000493:pharmacokinetics; D004718:Saccharomycetales / Q000201:enzymology*; D013379:Substrate Specificity; D015003:Yeasts / Q000201:enzymology*
D002413:Cations, Divalent; D008345:Manganese; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D008274:Magnesium