Pregled bibliografske jedinice broj: 16589
MITOCHONDRIAL AND CYTOPLASMIC SERYL-tRNA SYNTHETASES FROM Zea mays
MITOCHONDRIAL AND CYTOPLASMIC SERYL-tRNA SYNTHETASES FROM Zea mays // EMBO Workshop on Structure and Function of Aminoacyl-tRNA Synthetases / Florantz, Catherine (ur.).
Strasbourg: IBMC, 1998. (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 16589 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
MITOCHONDRIAL AND CYTOPLASMIC
SERYL-tRNA SYNTHETASES FROM Zea mays
Autori
Rokov, Jasmina ; Lenhard, Boris ; Filipić, Sanda ; Mijaković, Ivan ; Weygand-Đurašević, Ivana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
EMBO Workshop on Structure and Function of Aminoacyl-tRNA Synthetases
/ Florantz, Catherine - Strasbourg : IBMC, 1998
Skup
EMBO Workshop on Structure and Function of Aminoacyl-tRNA Synthetases
Mjesto i datum
Mittelwihr, Francuska, 10.10.1998. - 15.10.1998
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aminoacyl-tRNA synthetases; tRNA
Sažetak
In order to analyze the structure/function relationships among cytoplasmic and organellar seryl-tRNA synthetases (SerRS), we have characterized two Zea mays cDNAs. One encodes a protein (SerZMc) with significant similarity to other eukaryotic cytoplasmic SerRS enzymes, while the translation product of the other gene (SerZMm) is more similar to prokaryotic SerRSs.
Phylogenetic analyses have revealed that mitochondrial seryl-tRNA synthetases are evolutionary distant from the cytosolic enzymes. The two known mitochondrial SerRS sequences, from yeast (SerSCm) and maize (SerZMm), form a marginally significant clade, apparently due to increased mutation rate observed in most proteins with mitochondrial function.
To demonstrate the functional identity of SerZMm, the gene sequence encoding the putative mature protein was used for in vivo complementation of a temperature-sensitive Escherichia coli serS mutant. Additionally, Saccharomyces cerevisiae respiratory defficient strain, obtained by SerSCm gene disruption, was tested for complementation with a gene fusion, consisting of the proposed yeast SerSCm mitochondrial targeting signal and mature SerZMm.
The mature SerZMm protein overexpressed in E. coli efficiently aminoacylated bacterial tRNASer, while yeast tRNA was a poor substrate. Current studies are aimed at defining the differences in substrate specificities between cytoplasmic and organellar seryl-tRNA synthetases.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
119411
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb
Profili:
Ivana Weygand Đurašević
(autor)
Ivan Mijaković
(autor)
Jasmina Rokov Plavec
(autor)
Boris Lenhard
(autor)