Carboxypeptidase S- and Carboxypeptidase Y-Deficient Mutants of Saccharomyces cerevisiae
Carboxypeptidase S- and Carboxypeptidase Y-Deficient Mutants of Saccharomyces cerevisiae
复制标题
酿酒酵母羧肽酶 S 和羧肽酶 Y 缺陷突变体
作者：
D. Wolf;C. Ehmann
从一株缺乏羧肽酶Y的酿酒酵母（Saccharomyces cerevisiae）中发现了一种新的羧肽酶（羧肽酶S）。H.沃尔夫和U。Weiser，Eur. 73：553-556，1977）。从也缺乏羧肽酶Y的突变株中分离出缺乏羧肽酶S活性的突变株。对4个突变体进行了详细的分析，并将其归入一个互补组。在减数分裂的四分体中，该缺陷以2：2的比例分离。基因剂量实验表明，突变可能存在于羧肽酶S的结构基因中。两种酶，羧肽酶Y和S的情况下，不影响有丝分裂的生长。Aspocore形成只有轻微的影响，两个羧肽酶的情况下。在缺乏羧肽酶Y和S的情况下，营养剥夺条件下和孢子形成条件下的蛋白质降解没有明显的变化。当将导致蛋白酶B活性缺失并导致孢子形成部分减少的蛋白酶B突变引入缺乏两种羧肽酶的突变体中时，二倍体细胞形成孢子的能力几乎完全丧失。缺乏这两种羧肽酶的突变体不能在二肽苄氧基羰基甘氨酰-1-亮氨酸作为唯一氮源上生长，这表明羧肽酶Y和S在从外源肽供应营养物中具有额外的功能。果糖-1，6-二磷酸酶、胞质苹果酸脱氢酶和磷酸烯醇丙酮酸羧激酶的分解代谢物失活以及烟酰胺腺嘌呤二核苷酸磷酸依赖性谷氨酸脱氢酶的失活，这些被认为涉及体内蛋白水解的事件不依赖于羧肽酶Y和S的存在。在一个突变体缺乏这两种羧肽酶，四个新的蛋白水解酶与羧肽酶活性进行了检测。
A new carboxypeptidase (carboxypeptidase S) was found in a Saccharomyces cerevisiae strain lacking carboxypeptidase Y (D. H. Wolf and U. Weiser, Eur. J. Biochem. 73:553-556, 1977). Mutants devoid of carboxypeptidase S activity were isolated from a mutant strain that was also deficient in carboxypeptidase Y. Four mutants were analyzed in detail and fell into one complementation group. The defect segregated 2:2 in meiotic tetrads. Gene dosage experiments indicated that the mutation might reside in the structural gene of carboxypeptidase S. The absence of both enzymes, carboxypeptidases Y and S, did not affect mitotic growth. Ascopore formation was only slightly affected by the absence of both carboxypeptidases. Protein degradation under conditions of nutrient deprivation and under sporulation conditions showed no obvious alteration in the absence of carboxypeptidases Y and S. When a proteinase B mutation, which led to the absence of proteinase B activity and resulted in the partial reduction of sporulation, was introduced into a mutant lacking both carboxypeptidases, the ability of diploid cells to sporulate was nearly completely lost. Mutants lacking both carboxypeptidases were unable to grow on the dipeptide benzyloxycarbonylglycyl-l-leucine as a sole nitrogen source, which indicates an additional function for carboxypeptidases Y and S in supplying nutrients from exogenous peptides. Catabolite inactivation of fructose-1,6-bisphosphatase, cytoplasmic malate dehydrogenase, and phosphoenolpyruvate carboxykinase and inactivation of nicotin-amide adenine dinucleotide phosphate-dependent, glutamate dehydrogenase, events which have been proposed to involve proteolysis in vivo, were not dependent on the presence of carboxypeptidase Y and S. In a mutant lacking both carboxypeptidases, four new proteolytic enzymes with carboxypeptidase activity were detected.
酿酒酵母蛋白酶缺陷突变体中 NADP 依赖性谷氨酸脱氢酶的蛋白水解失活。
影响因子：
3.9
作者：
Hemmings,BA;Zubenko,GS;Jones,EW
通讯作者：
Jones,EW