多亚基蛋白质组装中的特异性。
Specificity in the assembly of multisubunit proteins.
作者信息
Cook R A, Koshland D E
出版信息
Proc Natl Acad Sci U S A. 1969 Sep;64(1):247-54. doi: 10.1073/pnas.64.1.247.
Abstract
The recoveries of activity in the presence of mixtures of several enzymes and a cellular debris were compared with the recoveries of the pure enzymes. In the acid-dissociation experiments, no interference from foreign proteins was observed nor were any cross hybrids between subunits of different enzymes found. This suggests that the intersubunit binding sites are highly specific and have been selected over evolutionary time for correct assembly. In the urea experiments, cross hybridization and decreased yields were observed in a few cases but in most cases the "foreign" unfolded chains did not influence the recovery of the test enzyme. The results suggest that compartmentalization, temporal or spatial, will not be required as far as assembly of subunits of cytoplasmic enzymes is concerned. The results suggest some cross reaction might occur if all peptide chains were unfolding together. If folding occurs during or immediately after translation, this difficulty would be avoided.
摘要
将几种酶与细胞碎片混合物存在时的活性回收率与纯酶的回收率进行了比较。在酸解离实验中，未观察到外来蛋白质的干扰，也未发现不同酶亚基之间的任何交叉杂交体。这表明亚基间结合位点具有高度特异性，并且在进化过程中已被选择用于正确组装。在尿素实验中，在少数情况下观察到了交叉杂交和产量降低，但在大多数情况下，“外来”的未折叠链并未影响测试酶的回收率。结果表明，就细胞质酶亚基的组装而言，不需要时间或空间上的区室化。结果表明，如果所有肽链一起展开，可能会发生一些交叉反应。如果折叠在翻译期间或翻译后立即发生，这种困难将得以避免。
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