Functional characterization of leucine-specific domain 1 from eukaryal and archaeal leucyl-tRNA synthetases

In early August, the research team led by Prof. Enduo Wang published their latest finding on Biochemical Journal - Functional characterization of leucine-specific domain 1 from eukaryal and archaeal leucyl-tRNA synthetases.

 

Leucyl-tRNA synthetase (LeuRS) catalyses the esterification oftRNAsLeu with leucine. This family of enzymes is dividedinto prokaryotic and eukaryal/archaeal groups according to the presence and position of specific insertions and extensions. In Prof. Wang’s study, the researchers investigated the function of LSD1 (leucinespecific domain 1), which is naturally present in eukaryal/archaeal LeuRSs, but absent from prokaryotic LeuRSs. When mutated in their common domain, the eukaryal and archaeal LeuRSs exhibited defects in the first reaction step of amino acid activationwith variations of leucine or ATP-binding strength, whereas the tRNA aminoacylation was moderately affected. When the eukaryal extension was mutated, severe tRNA charging defects were observed, suggesting that eukaryotes evolved this LSD1 extension in order to improve the aminoacylation reaction step. The results also showed that the LSD1s from organisms of both groups are dispensable for post-transfer editing. Together, the data promotes further understanding of the organization and structure of LeuRS domains.

 

This research was supported by the Ministry of Science and Technology, National Natural Science Foundation of China, Shanghai Municipal Commission for Science and Technology, and Chinese Academy of Sciences.