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An in vitro evolved precursor tRNA with aminoacylation activity
Author(s) -
Saito Hirohide,
Kourouklis Dimitrios,
Suga Hiroaki
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.7.1797
Subject(s) - ribozyme , biology , aminoacylation , transfer rna , rnase p , rna , vs ribozyme , base pair , t arm , amino acyl trna synthetases , protein biosynthesis , translation (biology) , aminoacyl trna synthetase , biochemistry , genetics , messenger rna , dna , gene
A set of catalysts for aminoacyl‐tRNA synthesis is an essential component for translation. The RNA world hypothesis postulates that RNA catalysts could have played this role. Here we show an in vitro evolved precursor tRNA consisting of two domains, a catalytic 5′‐leader sequence and an aminoacyl‐acceptor tRNA. The 5′‐leader sequence domain selectively self‐charges phenylalanine on the 3′‐terminus of the tRNA domain. This cis ‐acting ribozyme is susceptible to RNase P RNA, generating the corresponding 5′‐leader segment and the mature tRNA. Moreover, the 5′‐leader segment is able to aminoacylate the mature tRNA in trans . Mutational studies have revealed that C 74 and C 75 at the tRNA aminoacyl‐acceptor end form base pairs with G71 and G70 of the trans ‐acting ribozyme. Such Watson–Crick base pairing with tRNA has been observed in RNase P RNA and 23S rRNA, suggesting that all three ribozymes use a similar mechanism for the recognition of the aminoacyl‐acceptor end. Our demonstrations indicate that catalytic precursor tRNAs could have provided the foundations for the genetic coding system in the proto‐translation system.