The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex.

ABSTRACT: Aminoacyl-tRNA synthetases (ARSs) play essential roles in protein biosynthesis as well as in other cellular processes, often using evolutionarily acquired domains. For possible cooperativity and synergistic effects, nine ARSs assemble into the multi-tRNA synthetase complex (MSC) with three scaffold proteins: aminoacyl-tRNA synthetase complex-interacting multifunctional proteins 1, 2 and 3 (AIMP1, AIMP2 and AIMP3). X-ray crystallographic methods were implemented in order to determine the structure of a ternary subcomplex of the MSC comprising aspartyl-tRNA synthetase (DRS) and two glutathione S-transferase (GST) domains from AIMP2 and glutamyl-prolyl-tRNA synthetase (AIMP2_GST and EPRS_GST, respectively). While AIMP2_GST and EPRS_GST interact v

SUBMITTER: Hahn H 

PROVIDER: S-EPMC6760448 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature