Mbonyi K, Thevelein J M
Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Belgium.
Biochim Biophys Acta. 1988 Sep 16;971(2):223-6. doi: 10.1016/0167-4889(88)90195-4.
Addition of glucose or related fermentable sugars to yeast cells grown on non-fermentable carbon sources, triggers a RAS-protein mediated cAMP signal which induces a protein phosphorylation cascade. The high-affinity glucose uptake system in yeast cells is known to be glucose-repressible and only functional in strains containing at least one active kinase. In strains containing point or disruption mutations in the SNF3 gene, which codes for the high-affinity glucose carrier, the glucose-induced cAMP signal is still present. This indicates that the previously demonstrated requirement of a functional kinase for the induction of the cAMP signal, does not reflect requirement of high-affinity sugar transport. It also indicates that the unknown glucose-repressible protein in the induction sequence of the RAS-mediated cAMP signal is not the high-affinity sugar carrier.
向在非发酵性碳源上生长的酵母细胞中添加葡萄糖或相关可发酵糖,会触发RAS蛋白介导的cAMP信号,该信号会诱导蛋白质磷酸化级联反应。已知酵母细胞中的高亲和力葡萄糖摄取系统是可被葡萄糖抑制的,并且仅在含有至少一种活性激酶的菌株中起作用。在编码高亲和力葡萄糖载体的SNF3基因中含有点突变或缺失突变的菌株中,葡萄糖诱导的cAMP信号仍然存在。这表明先前证明的诱导cAMP信号需要功能性激酶,并不反映高亲和力糖转运的需求。这也表明,RAS介导的cAMP信号诱导序列中未知的葡萄糖可抑制蛋白不是高亲和力糖载体。