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Fidelity of decoding by aminoacyl-tRNA synthetases


Weygand-Đurašević, Ivana
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)


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, 08-12.09.2002

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


Projekt / tema
0119650

Ustanove
Prirodoslovno-matematički fakultet, Zagreb

Profili:

Avatar Url Ivana Weygand Đurašević (autor)

Citiraj ovu publikaciju

Weygand-Đurašević, Ivana
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)
Weygand-Đurašević, I. (2002) Fidelity of decoding by aminoacyl-tRNA synthetases. U: Kaučič, V. & Mali, G. (ur.)1st Central European Conference "Chemistry towards Biology".
@article{article, author = {Weygand-\DJura\v{s}evi\'{c}, I.}, year = {2002}, pages = {37}, keywords = {aminoacyl-tRNA synthetases, tRNA, accuracy of protein synthesis}, title = {Fidelity of decoding by aminoacyl-tRNA synthetases}, keyword = {aminoacyl-tRNA synthetases, tRNA, accuracy of protein synthesis}, publisher = {Slovenian Chemical Society}, publisherplace = {Portoro\v{z}, Slovenija} }