File Download

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher


Myung, Kyungjae
Center for Genomic Integrity
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Full metadata record

DC Field Value Language
dc.citation.number 1 -
dc.citation.startPage 6732 -
dc.citation.title NATURE COMMUNICATIONS -
dc.citation.volume 13 - Chung, Scisung - Kang, Mi-Sun - Alimbetov, Dauren S. - Mun, Gil-Im - Yunn, Na-Oh - Kim, Yunjin - Kim, Byung-Gyu - Wie, Minwoo - Lee, Eun A. - Ra, Jae Sun - 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 - Myung, Kyungjae - Cho, Yunje - 2023-12-21T13:19:07Z - 2023-12-21T13:19:07Z - 2022-12-09 - 2022-11 -
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. -
dc.identifier.bibliographicCitation NATURE COMMUNICATIONS, v.13, no.1, pp.6732 -
dc.identifier.doi 10.1038/s41467-022-34612-y -
dc.identifier.issn 2041-1723 -
dc.identifier.scopusid 2-s2.0-85141589378 -
dc.identifier.uri -
dc.identifier.wosid 000885370100014 -
dc.language 영어 -
dc.publisher NATURE PORTFOLIO -
dc.title Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1 -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Multidisciplinary Sciences -
dc.relation.journalResearchArea Science & Technology - Other Topics -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus DEGRADATION -
dc.subject.keywordPlus LINK -
dc.subject.keywordPlus AMINOACYL-TRANSFER-RNA -
dc.subject.keywordPlus TUMOR-SUPPRESSOR -
dc.subject.keywordPlus DNA-REPAIR -
dc.subject.keywordPlus COMPLEX -
dc.subject.keywordPlus RESECTION -
dc.subject.keywordPlus UBIQUITIN -
dc.subject.keywordPlus CTIP -
dc.subject.keywordPlus TRANSLATION -


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