A new perspective on the 50-year old mystery of why phages encode their own tRNAs.

Chemical modifications near the tRNA anticodon and specific mRNA–tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.

Experimental evolution and systematic sequence analysis of transfer RNA genes reveal that anticodon mutations provide adaptive plasticity to the translation machinery.

Although the genetic code uses three DNA base pairs to encode one amino acid, it is surprisingly tolerant to four-base codons, which can be used to incorporate nine of the twenty amino acids without any protein engineering.

The glycine T-box riboswitch recognizes tRNAgly and senses its aminoacylation state by first interacting with the anticodon region and subsequently probing the 3' end of the ligand using both specific structural elements and conformational dynamics.

The messenger RNA encoding La-related protein-4 (LARP4) contains a short region of instability whose codon clusters are sensitive to low abundance tRNAs that when elevated increase LARP4 activity for poly(A) lengthening of ribosomal protein mRNAs and other mRNAs.

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

Biochemical and genome-wide analysis demonstrates that m¹G37 is important for tRNA aminoacylation and for the entire elongation cycle of protein synthesis.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.