Herrero P, Fernández R, Moreno F
Departmento de Biología Funcional, Universidad de Oviedo, Spain.
J Gen Microbiol. 1989 May;135(5):1209-16. doi: 10.1099/00221287-135-5-1209.
The HXK2 gene product has an important role in controlling carbon catabolite repression in Saccharomyces cerevisiae. We have raised specific antibodies against the hexokinase PII protein and have demonstrated that it is a 58 kDa phosphoprotein with protein kinase activity. The predicted amino acid sequence of the HXK2 gene product has significant homology to the conserved catalytic domain of mammalian and yeast protein kinases. Protein kinase activity was located in a different domain of the protein from the hexose-phosphorylating activity. The hexokinase PII protein level remained unchanged in P2T22D mutant cells (hxk1 HXK2 glk1) growing in a complex medium with glucose. The protein kinase activity of hexokinase PII is regulated by the glucose concentration of the culture medium. Exit from the carbon catabolite repression phase and entry into derepression phase may be controlled, in part, by modulation of the 58 kDa protein kinase activity by changes in cyclic AMP concentration.
HXK2基因产物在控制酿酒酵母中的碳分解代谢物阻遏方面发挥着重要作用。我们制备了针对己糖激酶PII蛋白的特异性抗体,并证明它是一种具有蛋白激酶活性的58 kDa磷蛋白。HXK2基因产物的预测氨基酸序列与哺乳动物和酵母蛋白激酶的保守催化结构域具有显著同源性。蛋白激酶活性位于该蛋白中与己糖磷酸化活性不同的结构域。在含有葡萄糖的复杂培养基中生长的P2T22D突变细胞(hxk1 HXK2 glk1)中,己糖激酶PII蛋白水平保持不变。己糖激酶PII的蛋白激酶活性受培养基葡萄糖浓度的调节。从碳分解代谢物阻遏阶段退出并进入去阻遏阶段可能部分受环磷酸腺苷浓度变化对58 kDa蛋白激酶活性的调节控制。