Deutscher M P
J Cell Biol. 1984 Aug;99(2):373-7. doi: 10.1083/jcb.99.2.373.
Aminoacyl-tRNA synthetases from eucaryotic cells generally are isolated as high molecular weight complexes comprised of multiple synthetase activities, and often containing other components as well. A model is proposed for the synthetase complex in which hydrophobic extensions on the proteins serve to maintain them in their high molecular weight form, but are not needed for catalytic activity. The structural similarity of these enzymes to certain membrane-bound proteins, and its implications for synthetase localization and function in vivo, are discussed.
真核细胞中的氨酰-tRNA合成酶通常以高分子量复合物的形式被分离出来，这些复合物由多种合成酶活性组成，并且常常还含有其他成分。本文提出了一个关于合成酶复合物的模型，其中蛋白质上的疏水延伸部分有助于将它们维持在高分子量形式，但催化活性并不需要这些延伸部分。文中还讨论了这些酶与某些膜结合蛋白的结构相似性，以及这种相似性对合成酶在体内的定位和功能的影响。
