Naslov
Where translation meets plant steroid metabolism: interaction of seryl-tRNA synthetase and BEN1 protein from Arabidopsis thaliana

Autori
Kekez, Mario ; Zanki, Vladimir ; Kekez, Ivana ; Matković-Čalogović, Dubravka ; Rokov-Plavec, Jasmina

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

Izvornik
FEBS3+ From molecules to living systems / Dávid Szüts, Laszlo Buday - Veszprém : Federation of European Biochemical Societies (FEBS), 2018, 97-97

Skup
FEBS3+ conference "From molecules to living systems"

Mjesto i datum
Siófok, Mađarska, 02.09.2018. - 05.09.2018

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Podatak o recenziji nije dostupan

Ključne riječi
Seryl-tRNA synthetase ; BEN1 ; Arabidopsis thaliana ; protein translation ; plant steroid metabolism

Sažetak
Aminoacyl-tRNA synthetases (aaRS) enable translation by adding appropriate amino acids to cognate tRNAs. Charged tRNA molecules are directed to ribosome where the amino acid can be incorporated into a growing peptide, according to the genetic code. Additionally, aaRS can be functionaly involved in diverse cellular processes, independently or by interacting with other cellular proteins. Understanding this non- canonical nature of aaRS broadens our knowledge of proteomics and opens new functional perpectives in physiology. However, the studies of aaRS non-canonical functions and protein- protein interactions in plants are scarce. Therefore, our recent findings on the interaction of BEN1, a protein involved in the metabolism of brassinosteroid hormones, and cytosolic seryl- tRNA synthetase (SerRS) from plant Arabidopsis thaliana shed light on novel plant aaRS functions beyond translation. We detected SerRS:BEN1 complex in vivo using the yeast-2-hybrid screen and quantified the binding affinity by using surface plasmon resonance (SPR) and microscale thermophoresis (MST). To gain more insight into the interaction interface of the SerRS:BEN1 complex we solved the crystal structure of SerRS, being the first crystallographic structure of any plant aaRS known to date. We designed and prepared truncated variants of SerRS as well as BEN1 protein and analyzed them using MST. We demonstrated that the interaction depends on the central part of SerRS that contains the globular catalytic domain and the N-terminal extension of BEN1 protein. Our research of the interaction between SerRS and BEN1 shows a previously unreported functional link between protein translation and steroid metabolic pathways of the plant cell.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA