Alteration in protein kinase(s) level affects the phospholipid content in M. gypseum with modulated levels of calcium/cyclic AMP.

Protein kinase(s) have been identified for the first time in Microsporum gypseum. It phosphorylated exogenous protein acceptors preferentially histone IIs and casein and are mainly localized in the cytosolic fraction of M. gypseum. Alterations in protein kinase activity was observed in calcium/aminophylline and atropine (cAMP modulators) grown cells which is due to the modulation in the Ca2+/cAMP levels. Alteration in the protein kinase(s) activity finally affected the total phospholipid content in these modulated cells of M. gypseum. These observations suggest a correlation between the activity of protein kinase(s) and phospholipid synthesis in M. gypseum. This protein kinase(s) has a broad substrate specificity and is a seryl-threonyl type protein kinase(s) as it phosphorylates exogenous (histone) and endogenous proteins at serine and threonine residues.