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

Hyunggu Hahn, Sang Ho Park, Hyun Jung Kim, Sunghoon Kim, Byung Woo Han

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 (AIMP2GST and EPRSGST, respectively). While AIMP2GST and EPRSGST interact via conventional GST heterodimerization, DRS strongly interacts with AIMP2GST via hydrogen bonds between the α7-β9 loop of DRS and the β2-α2 loop of AIMP2GST, where Ser156 of AIMP2GST is essential for the assembly. Structural analyses of DRS-AIMP2GST-EPRSGST reveal its pivotal architecture in the MSC and provide valuable insights into the overall assembly and conditionally required disassembly of the MSC.

Original languageEnglish
Pages (from-to)958-967
Number of pages10
JournalIUCrJ
Volume6
DOIs
Publication statusPublished - 2019 Sep 1

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry
  • Materials Science(all)
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex'. Together they form a unique fingerprint.

  • Cite this