苯丙氨酰 - tRNA合成酶和异亮氨酰 - tRNA苯丙氨酸：一种氨酰 - tRNA的可能验证机制。
Phenylalanyl-tRNA synthetase and isoleucyl-tRNA Phe : a possible verification mechanism for aminoacyl-tRNA.
作者信息
Yarus M
出版信息
Proc Natl Acad Sci U S A. 1972 Jul;69(7):1915-9. doi: 10.1073/pnas.69.7.1915.
Abstract
The synthesis of isoleucyl-tRNA(Phe) (Escherichia coli) proceeds at an appreciable rate under normal in vitro conditions in the presence of isoleucyl-tRNA synthetase (EC 6.1.1.5) from E. coli. The misacylated product is shown here to be hydrolyzed by highly purified phenylalanyl-tRNA synthetase from E. coli, with release of isoleucine and active tRNA(Phe). Thus, phenylalanyl-tRNA synthetase possesses a previously unrecognized activity, which deacylates a mistakenly acylated tRNA(Phe); the enzyme is inactive toward correctly matched aminoacyl tRNAs. Such a mechanism could serve to verify aminoacyl-tRNAs, deacylating those that are misacylated. Thus, a common generalization needs to be modified: an amino acid is not necessarily committed to a given (incorrect) anticodon when it is incorporated into aminoacyl-tRNA. It may be possible to correct it thereafter.
摘要
在正常的体外条件下，在来自大肠杆菌的异亮氨酰 - tRNA合成酶（EC 6.1.1.5）存在时，异亮氨酰 - tRNA（苯丙氨酸）（大肠杆菌）的合成以可观的速率进行。此处显示，错误酰化的产物可被来自大肠杆菌的高度纯化的苯丙氨酰 - tRNA合成酶水解，释放出异亮氨酸和活性tRNA（苯丙氨酸）。因此，苯丙氨酰 - tRNA合成酶具有一种先前未被认识到的活性，即它能使错误酰化的tRNA（苯丙氨酸）脱酰基；该酶对正确配对的氨酰tRNA没有活性。这样一种机制可能有助于验证氨酰tRNA，使那些错误酰化的氨酰tRNA脱酰基。因此，一个常见的普遍观点需要修正：当氨基酸被掺入氨酰tRNA时，它不一定就与给定的（错误的）反密码子固定下来了。此后有可能对其进行校正。
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