Related Researcher

Author's Photo

Myung, Kyungjae
Center for Genomic Integrity
Research Interests
  • DNA Replication, DNA Repair, DNA Recombination, DNA Damage Response, cancer, aging

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

DC Field Value Language Chung, Scisung ko Kang, Mi-Sun ko Alimbetov, Dauren S. ko Mun, Gil-Im ko Yunn, Na-Oh ko Kim, Yunjin ko Kim, Byung-Gyu ko Wie, Minwoo ko Lee, Eun A. ko Ra, Jae Sun ko Oh, Jung-Min ko Lee, Donghyun ko Lee, Keondo ko Kim, Jihan ko Han, Seung Hyun ko Kim, Kyong-Tai ko Chung, Wan Kyun ko Nam, Ki Hyun ko Park, Jaehyun ko Lee, ByungHoon ko Kim, Sunghoon ko Zhao, Weixing ko Ryu, Sung Ho ko Lee, Yun-Sil ko Myung, Kyungjae ko Cho, Yunje ko 2022-12-23T04:45:44Z - 2022-12-09 ko 2022-11 ko
dc.identifier.citation NATURE COMMUNICATIONS, v.13, no.1, pp.6732 ko
dc.identifier.issn 2041-1723 ko
dc.identifier.uri -
dc.description.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. ko
dc.language 영어 ko
dc.publisher NATURE PORTFOLIO ko
dc.title Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1 ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-85141589378 ko
dc.identifier.wosid 000885370100014 ko
dc.type.rims ART ko
dc.identifier.doi 10.1038/s41467-022-34612-y ko
Appears in Collections:
BME_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show simple item record


  • mendeley


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.