Scisung Chung, Mi-Sun Kang, Dauren S Alimbetov, Gil-Im Mun, Na-Oh Yunn, Yunjin Kim, Byung-Gyu Kim, Minwoo Wie, Eun A Lee, Jae Sun Ra, Jung-Min Oh, Donghyun Lee, Keondo Lee, Jihan Kim, Seung Hyun Han, Kyong-Tai Kim, Wan Kyun Chung, Ki Hyun Nam, Jaehyun Park, ByungHoon Lee, Sunghoon Kim, Weixing Zhao, Sung Ho Ryu, Yun-Sil Lee, Kyungjae Myung, Yunje Cho
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...
November 8, 2022: Nature Communications