Pregled bibliografske jedinice broj: 5746
Strutural and functional relationship among cytoplasmic and mitochondrial seryl-tRNA synthetases
Strutural and functional relationship among cytoplasmic and mitochondrial seryl-tRNA synthetases // 17th International tRNA Workshop / Yokoyama, Shigeyuki (ur.).
Chiba, Japan, 1997. str. 6-9 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 5746 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Strutural and functional relationship among cytoplasmic and mitochondrial seryl-tRNA synthetases
Autori
Lenhard, Boris ; Filipić, Sanda ; Rokov, Jasmina ; Landeka, Irena ; Soell, Dieter ; Weygand-Đurašević, Ivana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
17th International tRNA Workshop
/ Yokoyama, Shigeyuki - , 1997, 6-9
Skup
17th International tRNA Workshop
Mjesto i datum
Chiba, Japan, 10.05.1997. - 15.05.1997
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aminoacyl-tRNA synthetase; tRNA
Sažetak
The activities of two nuclearly encoded seryl-tRNA synthetases (SerRS) are required in different protein-synthesizing cell compartments of Saccharomyces cerevisiae. To investigate the mechanism of serylation, structural organization of the enzymes and the mode of substrate recognition, we have recently complemented our research on cytoplasmic enzyme by cloning and expression of the gene for mitochondrial seryl-tRNA synthetase. There is only 26 % similarity in the primary structure of two SerRS proteins. Determination of substrate binding domains by alignment guided mutagenesis, performed recently at cytoplasmic SerRS (Lenhard, B., Filipi}, S., Landeka, I., [krti}, I., Söll, D. and Weygand-\ura{evi}, I. (1997) J. Biol. Chem. 272, 1136-1141), has been extended to analyze the structure/function relationship in mitochondrial enzyme. This is of particular interest as the substrate specificities of these enzymes must differ sufficiently to foil confusion between organellar and cytoplasmic protein synthesis. The crystal structure of prokaryotic SerRS (Cusack, S., Yaremchuk, A., and Tukalo, M. (1996) EMBO J. 15, 2834-2842) allowed us to produce structural models for yeast seryl-tRNA synthatases and to place the mutations in a structural context. In conjunction with structural data for Thermus thermophilus SerRS, our kinetic experiments suggest that yeast cytoplasmic enzyme displays tRNA-dependent serine recognition, affected by the mutations in motif 2 loop residues. We are trying to elucidate whether mitochondrial SerRS structurally and functionally resembles its cytoplasmic counterpart.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
119411
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb
Profili:
Irena Landeka Jurčević
(autor)
Jasmina Rokov Plavec
(autor)
Boris Lenhard
(autor)
Ivana Weygand Đurašević
(autor)