Sierra M F, Tzagoloff A
Proc Natl Acad Sci U S A. 1973 Nov;70(11):3155-9. doi: 10.1073/pnas.70.11.3155.
A low-molecular-weight protein synthesized in yeast mitochondria was purified. The protein was identified as a component of the rutamycin-sensitive ATPase. The amino-acid composition of the purified protein shows an extremely large preponderance of nonpolar residues, which may account for its solubility in chloroform-methanol. Indirect evidence suggests that this component is involved in the conferral of rutamycin sensitivity and may also have a function in the assembly of the ATPase complex.
在酵母线粒体中合成的一种低分子量蛋白质被纯化。该蛋白质被鉴定为鲁塔霉素敏感ATP酶的一个组分。纯化蛋白质的氨基酸组成显示出非极性残基的极大优势,这可能解释了其在氯仿 - 甲醇中的溶解性。间接证据表明,该组分参与了鲁塔霉素敏感性的赋予,并且可能在ATP酶复合物的组装中也具有功能。