Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

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 () and Yunje Cho ()
Additional contact information
Scisung Chung: Pohang University of Science and Technology
Mi-Sun Kang: Institute for Basic Science (IBS)
Dauren S. Alimbetov: University of Texas Health San Antonio
Gil-Im Mun: Ewha Womans University
Na-Oh Yunn: Pohang University of Science and Technology
Yunjin Kim: Pohang University of Science and Technology
Byung-Gyu Kim: Institute for Basic Science (IBS)
Minwoo Wie: Institute for Basic Science (IBS)
Eun A. Lee: Institute for Basic Science (IBS)
Jae Sun Ra: Institute for Basic Science (IBS)
Jung-Min Oh: Pusan National University
Donghyun Lee: Pohang University of Science and Technology
Keondo Lee: Pohang University of Science and Technology
Jihan Kim: Pohang University of Science and Technology
Seung Hyun Han: Pohang University of Science and Technology
Kyong-Tai Kim: Pohang University of Science and Technology
Wan Kyun Chung: Pohang University of Science and Technology
Ki Hyun Nam: Korea University
Jaehyun Park: Pohang University of Science and Technology
ByungHoon Lee: Daegu Gyeongbuk Institute of Science and Technology (DGIST)
Sunghoon Kim: Yonsei University
Weixing Zhao: University of Texas Health San Antonio
Sung Ho Ryu: Pohang University of Science and Technology
Yun-Sil Lee: Ewha Womans University
Kyungjae Myung: Institute for Basic Science (IBS)
Yunje Cho: Pohang University of Science and Technology

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-34612-y

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