Aminoacyl-tRNA synthetases (aaRSs) are the enzymes normally responsible for the attachment of amino acids (aa) to tRNAs. Numerous paralogous proteins of aaRSs have been identified in a wide range of organisms, but the functions of most of these aaRS-like proteins are yet to be determined. In PNAS, the study by Mocibob et al. (1) identifies a paralog of seryl-tRNA synthetase that does not aminoacylate a tRNA, but instead, aminoacylates an aa carrier protein. This exciting discovery provides an unforeseen function for the aaRS architecture and also uncovers a possible evolutionary link between ribosome-catalyzed translation and nonribosomal peptide synthesis
Aminoacyl-tRNA synthetases are normally found in one of two mutually exclusive structural classes, t...
Protein synthesis requires the pairing of amino acids with tRNAs catalyzed by the aminoacyl-tRNA syn...
The genetic code can be interpreted during translation as 21 amino acids and three termination signa...
Aminoacyl-tRNA synthetases (aaRSs) are multidomain proteins that specifically attach amino acids to ...
The role of tRNA as the adaptor in protein synthesis has held an enduring fascination for molecular ...
Genome‐scale analyses have shown numerous functional duplications in the canonical translational mac...
Accurate aminoacyl‐tRNA synthesis is essential for correct translation of the genetic code in all or...
Monomethylamine methyltransferase of the archaeon Methanosarcina barkeri contains a rare amino acid,...
SUMMARY The aminoacyl-tRNA synthetases (AARSs) and their relationship to the genetic code are examin...
Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They...
Insertion of lysine during protein synthesis depends on the enzyme lysyl-tRNA synthetase (LysRS), wh...
Lysyl-tRNA synthesis is catalyzed by two unrelated families of aminoacyl-tRNA synthetases. In most b...
Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure bot...
An investigation of the role of tRNA in the catalysis of aminoacylation of Escherichia coli glutamin...
We have analyzed the evolution of recognition of tRNAsSer by seryl-tRNA synthetases, and compared it...
Aminoacyl-tRNA synthetases are normally found in one of two mutually exclusive structural classes, t...
Protein synthesis requires the pairing of amino acids with tRNAs catalyzed by the aminoacyl-tRNA syn...
The genetic code can be interpreted during translation as 21 amino acids and three termination signa...
Aminoacyl-tRNA synthetases (aaRSs) are multidomain proteins that specifically attach amino acids to ...
The role of tRNA as the adaptor in protein synthesis has held an enduring fascination for molecular ...
Genome‐scale analyses have shown numerous functional duplications in the canonical translational mac...
Accurate aminoacyl‐tRNA synthesis is essential for correct translation of the genetic code in all or...
Monomethylamine methyltransferase of the archaeon Methanosarcina barkeri contains a rare amino acid,...
SUMMARY The aminoacyl-tRNA synthetases (AARSs) and their relationship to the genetic code are examin...
Accurately aminoacylated tRNAs are an a priori requirement for translation of the genetic code. They...
Insertion of lysine during protein synthesis depends on the enzyme lysyl-tRNA synthetase (LysRS), wh...
Lysyl-tRNA synthesis is catalyzed by two unrelated families of aminoacyl-tRNA synthetases. In most b...
Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure bot...
An investigation of the role of tRNA in the catalysis of aminoacylation of Escherichia coli glutamin...
We have analyzed the evolution of recognition of tRNAsSer by seryl-tRNA synthetases, and compared it...
Aminoacyl-tRNA synthetases are normally found in one of two mutually exclusive structural classes, t...
Protein synthesis requires the pairing of amino acids with tRNAs catalyzed by the aminoacyl-tRNA syn...
The genetic code can be interpreted during translation as 21 amino acids and three termination signa...