Pregled bibliografske jedinice broj: 120159
Fidelity of decoding by aminoacyl-tRNA synthetases
Fidelity of decoding by aminoacyl-tRNA synthetases // 1st Central European Conference "Chemistry towards Biology" / Kaučič, Venčeslav ; Mali, Gregor (ur.).
Ljubljana: Slovenian Chemical Society, 2002. (pozvano predavanje, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 120159 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Fidelity of decoding by aminoacyl-tRNA synthetases
Autori
Weygand-Đurašević, Ivana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
1st Central European Conference "Chemistry towards Biology"
/ Kaučič, Venčeslav ; Mali, Gregor - Ljubljana : Slovenian Chemical Society, 2002
Skup
1st Central European Conference "Chemistry towards Biology"
Mjesto i datum
Portorož, Slovenija, 08.09.2002. - 12.09.2002
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
aminoacyl-tRNA synthetases; tRNA; accuracy of protein synthesis
Sažetak
Translation is the process by which the genetic information contained in mRNA is used to determine the sequential order of amino acids in a protein. The high level of translational fidelity in the cell is ensured by various types of quality control mechanisms, which are adapted to prevent or correct naturally occurring mistakes. Accurate aminoacyl-tRNA synthesis is mostly dependent on the specificity of the aminoacyl-tRNA synthetases, i.e. their ability to choose between competing structurally similar substrates. Our studies have revealed that accurate seryl-tRNA synthesis is accomplished via tRNA-assisted optimization of amino acid binding to the enzyme active site. Based on our recent kinetic data, a mechanism is proposed by which transient protein:RNA complex activates the cognate amino acid more efficiently and more specifically than the apoenzyme alone. This may proceed via a tRNA-induced conformational change in the enzyme&#8217 ; s active site. SerRS enzymes slightly misactivate structurally similar threonine, but the formation of erroneous threonyl-adenylate is reduced in the presence of tRNASerCC. Thus, the sequence-specific tRNA:SerRS interactions enhance the accuracy of amino acid recognition, making corrective mechanisms unnecessary. In addition, it seems that the quality of seryl-tRNA formation may be improved by the complex formation between SerRS and a nonsynthetase protein. Potential biological relevance of the interaction between yeast SeRS and peroxin Pex21p, which has been identified in yeast, will be discussed.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
POVEZANOST RADA
Projekti:
0119650
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb
Profili:
Ivana Weygand Đurašević
(autor)