Original scientific paper

Efficiently Activated Serine Analogue is Not Transferred to Yeast tRNASer

Ita Gruić-Sovulj ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Morana Dulić ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Jelena Jarić ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Nevena Cvetešić ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Kristina Majsec ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Ivana Weygand-Đurašević ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia

Abstract

Covalent attachment of cognate amino acid to the cognate tRNA is a prerequisite for the faithful synthesis of proteins in the cell. Aminoacylation of tRNA, catalyzed by aminoacyl-tRNA synthetases
(aaRSs), proceeds by a two-step reaction whereby amino acid is first activated and then transferred to the 3'-ribose of tRNA. Serine hydroxamate (SerHX) is an interesting analogue of serine as it exhibits antimicrobial activity due to its inhibition of serylation in yeast and Escherichia coli. SerHX also mimics a noncognate substrate of yeast seryl-tRNA synthetase (ScSerRS) since it is efficiently activated and edited by this enzyme. However, whether this analogue is also transferred to tRNA during the second step of aminoacylation was not previously known. Here we show, for the first time, that aminoacylation of yeast tRNA with SerHX does not occur at a measurable rate, suggesting that the transfer is less tolerable toward SerHX than the activation step.

Keywords

serine hydroxamate; seryl-tRNA synthetase; tRNA; transfer step; amino acid activation

Hrčak ID:

56019

URI

https://hrcak.srce.hr/56019

Publication date:

15.7.2010.

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