Pregled bibliografske jedinice broj: 622393
Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli
Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli // Croatica chemica acta, 86 (2013), 1; 73-82 doi:10.5562/cca2173 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 622393 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Lack of discrimination against non-proteinogenic amino acid norvaline by elongation factor Tu from Escherichia coli
Autori
Cvetešić, Nevena ; Akmačić, Irena ; Gruić-Sovulj, Ita
Izvornik
Croatica chemica acta (0011-1643) 86
(2013), 1;
73-82
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
EF-Tu; norvaline; non-proteinogenic amino acids; aminoacyl-tRNA synthetases; leucyl-tRNA synthetase; mistranslation
Sažetak
The GTP-bound form of elongation factor Tu (EF-Tu) brings aminoacylated tRNAs (aa-tRNA) to the A-site of the ribosome. EF-Tu binds all cognate elongator aa-tRNAs with highly similar affinities, and its weaker or tighter binding of misacylated tRNAs may discourage their participation in translation. Norvaline (Nva) is a non-proteinogenic amino acid that is activated and transferred to tRNALeu by leucyl-tRNA synthetase (LeuRS). No notable accumulation of Nva-tRNALeu has been observed in vitro, because of the efficient post-transfer hydrolytic editing activity of LeuRS. However, incorporation of norvaline into proteins in place of leucine does occur under certain conditions in vivo. Here we show that EF-Tu binds Nva-tRNALeu and Leu-tRNALeu with similar affinities, and that Nva-tRNALeu and Leu-tRNALeu dissociate from EF-Tu at comparable rates. The inability of EF-Tu to discriminate against norvaline may have driven evolution of highly efficient LeuRS editing as the main quality control mechanism against misincorporation of norvaline into proteins.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
POVEZANOST RADA
Projekti:
119-0982913-1358 - Strukturna raznolikost seril-tRNA sintetaza i točnost biosinteze proteina (Rokov Plavec, Jasmina; Weygand Đurašević, Ivana, MZOS ) ( CroRIS)
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb
