Fernández-Bañares I, Clotet J, Ariño J, Guinovart J J
Departament de Bioquímica i Biologia Molecular, Facultat de Veterinària, Universitat Autònoma de Barcelona, Spain.
FEBS Lett. 1991 Sep 23;290(1-2):38-42. doi: 10.1016/0014-5793(91)81220-3.
The mechanism by which yeast ras2 mutant hyperaccumulates glycogen has been investigated. Total glycogen synthase activity was between 2.5 and 1.3 times higher in the ras2 mutant than in an isogenic strain. In addition, while in the normal strain the glycogen synthase activation state decreased along the exponential phase, in the mutant strain the opposite behaviour was observed: glycogen synthase activation state rose continuously reaching full activation at the beginning of the stationary phase. Glycogen phosphorylase a activity was up to 40 times higher in the mutant than in the normal strain. Glucose 6-phosphate and fructose 2,6-bisphosphate levels were slightly more elevated in the mutants. The increase in total glycogen synthase and, particularly, the full activation of this enzyme may explain glycogen hyperaccumulation in the ras2 mutant even in the presence of elevated levels of glycogen phosphorylase a.
人们已经对酵母ras2突变体过度积累糖原的机制进行了研究。ras2突变体中糖原合酶的总活性比同基因菌株高2.5至1.3倍。此外,在正常菌株中,糖原合酶的激活状态在指数生长期会下降,而在突变菌株中则观察到相反的情况:糖原合酶的激活状态持续上升,在稳定期开始时达到完全激活。突变体中糖原磷酸化酶a的活性比正常菌株高40倍。突变体中6-磷酸葡萄糖和2,6-二磷酸果糖的水平略有升高。即使在糖原磷酸化酶a水平升高的情况下,总糖原合酶的增加,尤其是该酶的完全激活,可能解释了ras2突变体中糖原的过度积累。