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Seryl-tRNA Synthetases: Enzymes with Multiple Personalities

Croatian Chemical Society
Publication Date
  • Seryl-Trna Synthetase
  • Transfer Rna
  • Synthetase Crystal Structure
  • Synthetase: Trna Model
  • Biology
  • Chemistry
  • Medicine


Seryl-tRNA synthetases (SerRS) are essential enzymes responsible for aminoacylation of cognate transfer-RNAs (tRNAsSer) with serine, which is then incorporated into the proteins being synthesized on the ribosome. Although tRNA synthetases are usually a very conserved class of enzymes, phylogenic analyses revealed the existence of two distinct types of serine-charging enzymes; a standard or bacterial-type SerRS is found in the majority of organisms (prokaryotes, eukaryotes and archaea), while a highly diverged methanogenic-type SerRS is confined to the methanogenic archaea. We give a short overview on our recent biochemical and structural contributions to the understanding of different molecular mecha-nisms of tRNA serylation.

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