Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Cell Culture
SUBMITTER: Byung-gyu kim
LAB HEAD: Yunje Cho
PROVIDER: PXD031261 | Pride | 2023-03-11
REPOSITORIES: Pride
Chung Scisung S Kang Mi-Sun MS Alimbetov Dauren S DS Mun Gil-Im GI Yunn Na-Oh NO Kim Yunjin Y Kim Byung-Gyu BG Wie Minwoo M Lee Eun A EA Ra Jae Sun JS Oh Jung-Min JM Lee Donghyun D Lee Keondo K Kim Jihan J Han Seung Hyun SH Kim Kyong-Tai KT Chung Wan Kyun WK Nam Ki Hyun KH Park Jaehyun J Lee ByungHoon B Kim Sunghoon S Zhao Weixing W Ryu Sung Ho SH Lee Yun-Sil YS Myung Kyungjae K Cho Yunje Y
Nature communications 20221108 1
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 interac ...[more]