MacKelvie S H, Andrews P D, Stark M J
Department of Biochemistry, University of Dundee, United Kingdom.
Mol Cell Biol. 1995 Jul;15(7):3777-85. doi: 10.1128/MCB.15.7.3777.
In higher eukaryotes, the activity and specificity of the type 1 protein serine-threonine phosphatase (PP1) catalytic subunit is thought to be controlled by its association with a number of regulatory or targeting subunits. Here we describe the characterization of a gene encoding one such potential polypeptide in the yeast Saccharomyces cerevisiae. The gene which we have isolated (termed SDS22) encodes a product with a high degree of sequence identity to the fission yeast sds22 protein, a known regulator of the mitotic function of PP1 in Schizosaccharomyces pombe. Using two different criteria, we have demonstrated that Sds22p and the catalytic subunit of PP1 (Glc7p) interact in yeast cells. We have also generated a temperature-sensitive allele of GLC7 (glc7-12) which causes a block to the completion of mitosis at the restrictive temperature. Additional copies of SDS22 lead to allele-specific suppression of the glc7-12 mutant, strongly suggesting that the interaction between the two proteins is of functional significance. Sds22p is therefore likely to be the second example of a PP1 regulatory subunit identified in S. cerevisiae.
在高等真核生物中,1型蛋白丝氨酸 - 苏氨酸磷酸酶(PP1)催化亚基的活性和特异性被认为是由其与多种调节或靶向亚基的结合所控制。在此,我们描述了酿酒酵母中一个编码此类潜在多肽的基因的特征。我们分离出的基因(称为SDS22)编码的产物与粟酒裂殖酵母中的sds22蛋白具有高度的序列同一性,sds22蛋白是粟酒裂殖酵母中PP1有丝分裂功能的已知调节因子。使用两种不同的标准,我们证明了Sds22p与PP1的催化亚基(Glc7p)在酵母细胞中相互作用。我们还产生了GLC7的温度敏感等位基因(glc7 - 12),该等位基因在限制温度下导致有丝分裂完成受阻。SDS22的额外拷贝导致glc7 - 12突变体的等位基因特异性抑制,强烈表明这两种蛋白质之间的相互作用具有功能意义。因此,Sds22p可能是酿酒酵母中鉴定出的PP1调节亚基的第二个例子。