Davis T N, Urdea M S, Masiarz F R, Thorner J
Cell. 1986 Nov 7;47(3):423-31. doi: 10.1016/0092-8674(86)90599-4.
Calmodulin was purified from Saccharomyces cerevisiae based on its characteristic properties. Like other calmodulins, the yeast protein is small, heat-stable, acidic, retained by hydrophobic matrices in a Ca2+-dependent manner, exhibits a pronounced Ca2+-induced shift in electrophoretic mobility, and binds 45Ca2+. Using synthetic oligonucleotide probes designed from the sequences of two tryptic peptides derived from the purified protein, the gene encoding yeast calmodulin was isolated. The gene (designated CMD1) is a unique, single-copy locus, contains no introns, and resides on chromosome II. The amino acid sequence of yeast calmodulin shares 60% identity with other calmodulins. Disruption or deletion of the yeast calmodulin gene results in a recessive-lethal mutation; thus, calmodulin is essential for the growth of yeast cells.
基于其特性，从酿酒酵母中纯化出钙调蛋白。与其他钙调蛋白一样，酵母蛋白体积小、热稳定、呈酸性，以Ca2+依赖的方式被疏水基质保留，在电泳迁移率上表现出明显的Ca2+诱导的迁移变化，并能结合45Ca2+。利用从纯化蛋白衍生的两个胰蛋白酶肽段序列设计的合成寡核苷酸探针，分离出了编码酵母钙调蛋白的基因。该基因（命名为CMD1）是一个独特的单拷贝基因座，不含内含子，位于II号染色体上。酵母钙调蛋白的氨基酸序列与其他钙调蛋白有60%的同源性。酵母钙调蛋白基因的破坏或缺失会导致隐性致死突变；因此，钙调蛋白对酵母细胞的生长至关重要。
