Starzyk R M, Koontz S W, Schimmel P
Nature. 1982 Jul 8;298(5870):136-40. doi: 10.1038/298136a0.
A covalent adduct of an aminoacyl tRNA synthetase and uracil nucleoside has been isolated. The enzyme adduct is catalytically inactive; one nucleoside is bound per catalytic site. The release of uridine restores enzyme activity. The nucleoside attaches to a protein segment required for tRNA interaction. The findings add support to concepts of a covalent component for some protein-nucleic acid complexes.
已分离出一种氨酰tRNA合成酶与尿嘧啶核苷的共价加合物。该酶加合物无催化活性;每个催化位点结合一个核苷。尿苷的释放可恢复酶活性。该核苷附着于tRNA相互作用所需的蛋白质片段上。这些发现为某些蛋白质 - 核酸复合物存在共价成分的概念提供了支持。