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Mi Sun, Kang
유전체 항상성 연구단
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Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1

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Title
Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1
Author(s)
Chung, Scisung; Mi-Sun Kang; Alimbetov, Dauren S.; Mun, Gil-Im; Yunn, Na-Oh; Kim, Yunjin; Byung-Gyu Kim; Minwoo Wie; Eun A. Lee; Jae Sun Ra; Oh, Jung-Min; Lee, Donghyun; Lee, Keondo; Kim, Jihan; Han, Seung Hyun; Kim, Kyong-Tai; Chung, Wan Kyun; Nam, Ki Hyun; Park, Jaehyun; Lee, ByungHoon; Kim, Sunghoon; Zhao, Weixing; Ryu, Sung Ho; Lee, Yun-Sil; Kyungjae Myung; Cho, Yunje
Publication Date
2022-11
Journal
NATURE COMMUNICATIONS, v.13, no.1
Publisher
NATURE PORTFOLIO
Abstract
Aminoacyl-tRNA synthetases possess unique domains. In this study the structure of the vertebrate IARS1 and EARS1 complex reveals that vertebrate IARS1 protects the DNA repair factor BRCA1 from proteolytic degradation via its UBX-fold domain. 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.
URI
https://pr.ibs.re.kr/handle/8788114/12582
DOI
10.1038/s41467-022-34612-y
ISSN
2041-1723
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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