Kal'nov S L, Serebriakova N V, Zubatov A S, Luzikov V N
Biokhimiia. 1978;43(4):662-8.
Products of mitochondrial protein synthesis were specifically labeled with 3H-leucine in the presence of cycloheximide at the end of the exponential phase of yeast aerobic growth on glucose. The mitochondria isolated from these cells lost 37-40% of the label from the protein fraction during 60 min incubation at 35 degrees, which was accompanied by the accumulation of 3H-leucine in TCA-soluble fraction. This process was suppressed by phenyl-methyl sulfonyl fluoride and p-chloromercuriphenyl sulfonate, the inhibitors of proteases, and could thus be considered as the proteolysis of the products of mitochondrial protein synthesis. The proteolysis was ATP dependent and was stimulated by puromycine which is known to induce the removal of incomplete polypeptides from mitochondrial ribosomes. A body of indirect evidence allows a suggestion to be made that the observed proteolysis can hardly be due to the action of cytoplasmic proteinases.
在葡萄糖上进行酵母有氧生长指数期结束时，在放线菌酮存在的情况下，用³H-亮氨酸对线粒体蛋白质合成产物进行特异性标记。从这些细胞中分离出的线粒体在35℃孵育60分钟期间，蛋白质部分的标记损失了37 - 40%，同时³H-亮氨酸在三氯乙酸可溶性部分积累。这个过程被蛋白酶抑制剂苯甲基磺酰氟和对氯汞苯磺酸盐所抑制，因此可以被认为是线粒体蛋白质合成产物的蛋白水解。蛋白水解依赖于ATP，并受到嘌呤霉素的刺激，已知嘌呤霉素可诱导从不完全多肽中去除线粒体核糖体。大量间接证据表明，观察到的蛋白水解几乎不可能是由于细胞质蛋白酶的作用。
