Naslov
Aminoacyl-tRNA synthetase complex in methanogenic archaea

Autori
Godinić-Mikulčić, Vlatka ; Jarić, Jelena ; Ibba, Michael ; Weygand-Đurašević, Ivana

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
EMBO Young Scientists Forum: Book of Abstracts / - , 2009, 20-20

Skup
EMBO Young Scientists Forum

Mjesto i datum
Zagreb, Hrvatska, 15.06.2009. - 17.06.2009

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
seryl-tRNA synthetase ; multi-synthetase complexes ; yeast two-hybrid ; protein-protein interactions

Sažetak
Seryl-tRNA synthetases are esential enzymes for protein biosynthesis. Moreover, an elaborate network of protein-protein interactions of aminacyl-tRNA synthetases is required for efficient translation in all domains of life. Several aminoacyl-tRNA synthetases (aaRS) are located in multi-synthetase complexes (MSC) in mammals. Identification of the network that connects possible regulatory non-synthetase proteins to synthetases or synthetases to each other and to the cellular processes they affect is a critical need. Archael SerRSs diverge into two major and disparate types of enzymes (bacterial and methanogenic type). We revealed protein partners of methanogenic type seryl-tRNA synthetase (SerRS) in Methanothermobacter thermautotrophicus using yeast two-hybrid screen that facilitates construction of protein– protein linkage maps. M. thermautrophicus arginyl-tRNA synthetase (ArgRS) was found interacting with SerRS as a result of the screen. We have isolated and kinetically examined M. thermautotrophicus SerRS to gain biochemical insight into the complex. Further, dissociation constant of SerRS:ArgRS complex was determined by surface plasmon resonance. Interestingly, the biological significance of interaction SerRS with ArgRS is improvement of SerRS enzymatic activity two- to five-fold. Before, SerRS has never been found interacting with another synthetase or within the MSC. This type of structural organization is not restricted to eukaryotic species because archaeal requirements for aaRS associations are becoming more evident, as these proteins can function together in many important biological contexts such as translation and substrate channeling.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA