Efficiently Activated Serine Analogue is Not Transferred to Yeast tRNASer

Gruić-Sovulj, Ita and Dulić, Morana and Jarić, Jelena and Cvetešić, Nevena and Majsec, Kristina and Weygand-Đurašević, Ivana (2010) Efficiently Activated Serine Analogue is Not Transferred to Yeast tRNASer. Croatica Chemica Acta, 83 (2). pp. 163-169. ISSN 0011-1643

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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.

Item Type: Article
Keywords: serine hydroxamate, seryl-tRNA synthetase, tRNA, transfer step, amino acid activation
Date: 2010
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Faculty of Science > Department of Chemistry
Publisher: Hrvatsko kemijsko društvo
Related URLs:
Depositing User: mag. bibl. Ana Šafran
Date Deposited: 09 May 2014 10:31
Last Modified: 09 May 2014 10:31
URI: http://digre.pmf.unizg.hr/id/eprint/1089

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