Pregled bibliografske jedinice broj: 777135
Probing protein:nucleic acid interactions by microscale thermophoresis: a case of aminoacyl- tRNA synthetase and tRNA
Probing protein:nucleic acid interactions by microscale thermophoresis: a case of aminoacyl- tRNA synthetase and tRNA // Book of Abstracts of the Symposium and Workshop on Microscale Thermophoresis / Godinić Mikulčić, Vlatka ; Sviben, Igor ; Rokov-Plavec, Jasmina (ur.).
Zagreb: Prirodoslovno-matematički fakultet Sveučilišta u Zagrebu, 2015. str. 12-12 (predavanje, nije recenziran, sažetak, znanstveni)
CROSBI ID: 777135 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Probing protein:nucleic acid interactions by microscale thermophoresis: a case of aminoacyl- tRNA synthetase and tRNA
Autori
Dulić, Morana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Book of Abstracts of the Symposium and Workshop on Microscale Thermophoresis
/ Godinić Mikulčić, Vlatka ; Sviben, Igor ; Rokov-Plavec, Jasmina - Zagreb : Prirodoslovno-matematički fakultet Sveučilišta u Zagrebu, 2015, 12-12
ISBN
978-953-6076-37-6
Skup
Symposium and Workshop on Microscale Thermophoresis
Mjesto i datum
Zagreb, Hrvatska, 30.06.2015. - 01.07.2015
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Nije recenziran
Ključne riječi
Leucyl-tRNA synthetase; deacylation; editing; specificity; microscale thermophoresis
Sažetak
Aminoacyl-tRNA synthetases (aaRSs) covalently pair cognate amino acid and cognate tRNA in an ATP- dependent manner. Due to structural similarity among different amino acids, some aaRSs also catalyze synthetic reactions with noncognate amino acids. To maintain accuracy of translation, these aaRSs have evolved proofreading mechanisms. The more widespread mechanism is hydrolysis of noncognate aminoacyl-adenylate called pre-transfer editing, occurring in the synthetic site. More efficient mechanism is post-transfer editing or deacylation of mischarged tRNA, which is occurring in a separate domain. To prevent futile ATP consumption, the deacylation domain efficiently discriminates against cognate charged tRNA. Here we explored interaction of leucyl-tRNA synthetase (LeuRS) with uncharged tRNALeu as its substrate and further with cognate and noncognate charged tRNA (Leu- tRNALeu and NvatRNALeu), which are products of synthetic reactions, but substrates for the hydrolytic reaction by LeuRS. Microscale themophoresis was valuable tool for studying these interactions due to its speed and requirement for small amount of material. Combining these results with the other thermodynamic and kinetic approaches demonstrated that substrate specificity in deacylation is predominately governed by the complementarity established at the transition state.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
