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Croatica Chemica Acta, Vol.82 No.2 July 2009.
Review article
Seryl-tRNA Synthetases: Enzymes with Multiple Personalities
Silvija Bilokapić
; Department of Chemistry, Faculty of Science, University of Zagreb, Zagreb, Croatia
Nenad Ban
; Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology, ETH Zürich, Switzerland
Ivana Weygand-Đurašević
; Department of Chemistry, Faculty of Science, University of Zagreb, Zagreb, Croatia
Fulltext: pdf (12 MB),
English,
Pages 493 - 501
,
Abstracts
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.
Keywords
seryl-tRNA synthetase; transfer RNA; synthetase crystal structure; synthetase: tRNA model
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