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

Abstract

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

Hrčak ID:

39697

URI

https://hrcak.srce.hr/39697

Publication date:

15.7.2009.

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