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Transfer RNAs (tRNAs) are a type of non-coding ribonucleic acid (ncRNA) that carry specific amino acids and recognize unique messenger RNA (mRNA) sequences. The pairing of a tRNA to its compatible mRNA sequence within the ribosome is the basis for the translation of RNA into protein.
An emerging therapeutic strategy is to suppress nonsense mutations with engineered suppressor tRNAs. Here, the authors show that the mRNA translation velocity is a key parameter determining the efficacy of suppressor tRNAs.
Precise protein synthesis is achieved by tRNA modifications. Here the authors revealed that modified cytidines in tRNAIle use their long side chains to make additional interactions with mRNA for stable tRNA binding on the ribosome.
Rybak and Gagnon elucidate the mechanism of AUG codon avoidance by the minor isoleucine tRNA in Escherichia coli. The lysidinylated C34 in the anticodon loop of tRNAIle weakens interactions with the mRNA and destabilizes the EF-Tu ternary complex.
Duan et al. demonstrate that the m2A modification is ubiquitous in plants and tRNA m2A37 promotes a relaxed conformation of tRNA, enhancing translation efficiency by facilitating decoding of tandem m2A-tRNA-dependent codons.
tRNA display enables the direct selection of orthogonal aminoacyl-tRNA synthetases that acylate orthogonal tRNAs with non-canonical monomers, enabling in vivo synthesis of proteins that include these monomers and expanding the repertoire of the genetic code.
Aminoacyl-tRNA synthetases translate the genetic code. These enzymes harbor signature catalytic motifs dating from their ancient ancestors. A natural variation of one of the stated motifs was discovered and linked to antibiotic hyper-resistance.
Protein translation is the ultimate paradigm for sequence-defined polymer synthesis. To introduce non-canonical monomers into the genetic code of living organisms, pairs of biomolecules known as aminoacyl-tRNA synthetases (aaRSs) and transfer RNAs (tRNAs) are required. The discovery and engineering of five such pairs, that do not interfere with each other or the aaRS–tRNA pairs of a bacterial host, sets the stage for highly modified genetically encoded biopolymers.
The RNA methyltransferase (MTase) METTL1 catalyzes N7-methylguanosine (m7G) modification at position 46 in human transfer RNAs (tRNAs). Its dysregulation drives tumorigenesis in many cancer types. Two papers now reveal the structural basis of this tRNA maturation event.
A new study in Science reports the refactoring of genetic codes in Escherichia coli to create a bidirectional ‘genetic firewall’ that prevents genetic transfer from or to synthetic organisms.
Thandapani et al. examined the role for tRNA biogenesis in T cell acute lymphoblastic leukaemia (T-ALL), and found that T-ALL cells are sensitive to valine tRNA levels, which could be exploited therapeutically by dietary valine restriction.
