Alexieva K I, Venkov P V
Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria.
Folia Microbiol (Praha). 2000;45(3):251-4. doi: 10.1007/BF02908954.
Saccharomyces cerevisiae strain MW11 is a temperature-sensitive mutant which exports twenty times more proteins at 37 degrees C than parental or wild-type strains do. To understand the mechanism underlying the protein overexport in the mutant the possibility of an altered cell-wall structure leading to facilitated release of cell-surface proteins was studied. Data on calcofluor white and zymolyase sensitivities, resistance to killer 1 toxin and determination of exported acid phosphatase and invertase did not provide evidence for alterations in the cell-wall structure that could explain the protein overexport phenotype. The results were obtained in experiments when transcription of mutated gene was discontinued which permits the full expression of the protein overexport phenotype.
酿酒酵母菌株MW11是一种温度敏感型突变体，在37摄氏度时输出的蛋白质比亲本菌株或野生型菌株多20倍。为了了解该突变体中蛋白质过度输出的潜在机制，研究了细胞壁结构改变导致细胞表面蛋白释放更容易的可能性。关于荧光增白剂和溶壁酶敏感性、对杀手1毒素的抗性以及输出的酸性磷酸酶和转化酶的测定的数据，没有提供可解释蛋白质过度输出表型的细胞壁结构改变的证据。这些结果是在突变基因转录停止的实验中获得的，这使得蛋白质过度输出表型得以充分表达。
