Naslov
Efficiently activated serine analogue is not transferred to yeast tRNASer

Autori
Gruić-Sovulj, Ita ; Dulić, Morana ; Jarić, Jelena ; Cvetešić, Nevena ; Majsec, Kristina ; Weygand-Đurašević, Ivana

Izvornik
Croatica chemica acta (0011-1643) 83 (2010), 2; 163-169

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

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

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA