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Publication Abstract from PubMed

Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.

Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.,Chung S, Kang MS, Alimbetov DS, Mun GI, Yunn NO, Kim Y, Kim BG, Wie M, Lee EA, Ra JS, Oh JM, Lee D, Lee K, Kim J, Han SH, Kim KT, Chung WK, Nam KH, Park J, Lee B, Kim S, Zhao W, Ryu SH, Lee YS, Myung K, Cho Y Nat Commun. 2022 Nov 8;13(1):6732. doi: 10.1038/s41467-022-34612-y. PMID:36347866^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.