In vitro phosphorylation of high molecular weight glutenin subunits from wheat endosperm | [Phosphorylation in vitro des sous-unites de glutenine a haut poids moleculaire extraites de l'endosperme de ble]
1999
Facchiano, A.M. (Second University of Naples (Italie). Research Center of Computational and Biotechnological Sciences) | Colonna, G. | Chiosi, E. | Illiano, G. | Spina, A. | Lafiandra, D. | Buonocore, F.
Francés. We have investigated the in vitro phosphorylation of high molecular weight glutenin subunits (HMW-GS), a group of non-soluble proteins present in wheat endosperm. Computer aided searches of potential biological sites in the known sequences of these proteins have evidenced the presence of sequence motifs specific for protein kinase C (PKC), calcium-dependent protein kinase from wheat, casein kinase II, tyrosine protein kinase and glycosylation. We have demonstrated that subunit lBx7 is a substrate of a partially purified PKC from rat brain. Further experiments have shown that this subunit is phosphorylated by an endogenous protein kinase activity found in wheat flour. These preliminary results are important for the possible implications on the structure-function relationships of these proteins and could probably suggest, for the first time, a potential physiological role in particular situations for some HMW-GS
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