Peng X X, Shih D S
J Biol Chem. 1984 Mar 10;259(5):3197-201.
The products of translation of cowpea mosaic virus B-RNA in rabbit reticulocyte lysates are proteolytically cleaved to form a specific set of proteins. The primary cleavage occurs as nascent peptide chains elongate to a size of about 150 kilodaltons yielding a 32K protein and, upon chain completion, a 170K protein. This cleavage reaction is inhibited by 3 mM iodoacetamide. The 170K protein, in turn, is cleaved to yield either of two pairs of proteins, a 110K and 60K pair or a 87K and 84K pair. The reaction for forming the 110K-60K pair is sensitive to dilution, indicating that a free factor is involved. The reaction for forming the 87K-84K pair, on the other hand, is not affected by diluting the lysate reaction mixture with buffer even to 200-fold, indicating that the reaction is autolytic. Formation of the 110K-60K pair, but not the 87K-84K pair, is inhibited by 2 mM zinc chloride. Translational mapping data indicate that the 87K and 60K proteins are derived from the NH2-terminal side of the 170K protein.
豇豆花叶病毒B-RNA在兔网织红细胞裂解物中的翻译产物经蛋白水解切割形成一组特定的蛋白质。初次切割发生在新生肽链延伸至约150千道尔顿大小时，产生一个32K蛋白，肽链合成完成后，产生一个170K蛋白。该切割反应受到3 mM碘乙酰胺的抑制。170K蛋白继而被切割，产生两对蛋白质中的一对，即110K和60K这一对，或87K和84K这一对。形成110K-60K对的反应对稀释敏感，表明涉及一个游离因子。另一方面，用缓冲液将裂解物反应混合物稀释至200倍，形成87K-84K对的反应也不受影响，表明该反应是自溶反应。2 mM氯化锌抑制110K-60K对的形成，但不抑制87K-84K对的形成。翻译图谱数据表明，87K和60K蛋白源自170K蛋白的氨基末端一侧。
