An aminoacylation ribozyme evolved from a natural tRNA-sensing T-box riboswitch.,Nature Chemical Biology

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An aminoacylation ribozyme evolved from a natural tRNA-sensing T-box riboswitch.
Nature Chemical Biology ( IF 12.9 ) Pub Date : 2020-03-23 , DOI: 10.1038/s41589-020-0500-6
Satoshi Ishida ₁ , Naohiro Terasaka ₁ , Takayuki Katoh ₁ , Hiroaki Suga ₁

Affiliation

When the primitive translation system first emerged in the hypothetical RNA world, ribozymes could have been responsible for aminoacylation. Given that naturally occurring T-box riboswitches selectively sense the aminoacylation status of cognate tRNAs, we introduced a domain of random sequence into a T-box-tRNA conjugate and isolated ribozymes that were self-aminoacylating on the 3'-terminal hydroxyl group. One of them, named Tx2.1, recognizes the anticodon and D-loop of tRNA via interaction with its stem I domain, similarly to the parental T-box, and selectively charges N-biotinyl-L-phenylalanine (Bio-lPhe) onto the 3' end of the cognate tRNA in trans. We also demonstrated the ribosomal synthesis of a Bio-lPhe-initiated peptide in a Tx2.1-coupled in vitro translation system, in which Tx2.1 catalyzed specific tRNA aminoacylation in situ. This suggests that such ribozymes could have coevolved with a primitive translation system in the RNA world.

中文翻译：

氨基酰化核酶从天然的tRNA感应T盒核糖开关进化而来。

当原始翻译系统首次出现在假设的RNA世界中时，核酶可能负责氨基酰化作用。鉴于天然存在的T-box核糖开关选择性地检测相关tRNA的氨基酰化状态，我们将随机序列结构域引入T-box-tRNA结合物中，并分离出在3'-末端羟基上被自身氨基酰化的核酶。其中一个名为Tx2.1，与亲本T-box类似，通过与其茎I结构域的相互作用识别tRNA的反密码子和D环，并选择性地将N-生物素-L-苯丙氨酸（Bio-Phe）充电到反式同源tRNA的3'端。我们还证明了在Tx2.1耦合的体外翻译系统中，Bio-lPhe引发的肽的核糖体合成，其中Tx2.1催化原位特异性的tRNA氨酰化。

更新日期：2020-04-24

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