Naslov
The interaction of yeast seryl-tRNA synthetase with the peroxin

Autori
Ročak, Sanda ; Godinić, Vlatka ; Landeka, Irena ; Weygand-Đurašević, Ivana

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
European Journal of Biochemistry / Wilkinson et al. - Oxford : Wiley-Blackwell, 2004, 93-93

Skup
29th Congress of the Feaderation of European Biochemical Societies (FEBS)

Mjesto i datum
Varšava, Poljska, 26.06.2004. - 01.07.2004

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
tRNASer ; seryl-tRNA synthetase ; protein cofactor

Sažetak
Peroxin Pex21p was identified as seryl-tRNA synthetase-interacting protein in Saccharomyces cerevisiae both in vivo and in vitro. Besides its main function in peroxisome biogenesis, Pex21p acts as specific activator of SerRS by increasing the efficiency of aminoacylation. In order to map SerRS/Pex21p interactive domains, several deletion mutants of SerRS have been produced. The interaction with peroxin was almost entirely lost after deleting positively charged C-terminal peptide of SerRS, which characterizes all eukariotyc seryl-tRNA synthetases. We have previously shown that such truncation also leads to toxicity in vivo, due to altered substrate recognition. These results suggest the involvement of Pex21p in stabilizing the conformation of SerRS active site, which could be important for maintaining the accuracy of serylation.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA