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Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.
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.
Affiliation
  • Chung S; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kang MS; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea.
  • Alimbetov DS; Department of Biochemistry and Structural Biology, University of Texas Health San Antonio, San Antonio, TX, 78229, USA.
  • Mun GI; Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul, Republic of Korea.
  • Yunn NO; Postech Biotech Center, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kim Y; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kim BG; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea.
  • Wie M; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea.
  • Lee EA; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea.
  • Ra JS; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea.
  • Oh JM; Department of Oral Biochemistry, School of Dentistry, Pusan National University, Pusan, Republic of Korea.
  • Lee D; Department of Mechanical Engineering, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Lee K; Department of Mechanical Engineering, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kim J; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Han SH; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kim KT; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Chung WK; Department of Mechanical Engineering, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Nam KH; Division of Biotechnology, Korea University, Seoul, Republic of Korea.
  • Park J; Institute of Life Science and Natural Resources, Korea University, Seoul, Republic of Korea.
  • Lee B; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Kim S; Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu, Republic of Korea.
  • Zhao W; Institute for Artificial Intelligence and Biomedical Research, College of Pharmacy, Gangnam Severance Hospital, Yonsei University, Incheon, 21983, Republic of Korea.
  • Ryu SH; Department of Biochemistry and Structural Biology, University of Texas Health San Antonio, San Antonio, TX, 78229, USA.
  • Lee YS; Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
  • Myung K; Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul, Republic of Korea.
  • Cho Y; Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, 44919, Republic of Korea. kmyung@ibs.re.kr.
Nat Commun ; 13(1): 6732, 2022 11 08.
Article in En | MEDLINE | ID: mdl-36347866
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Amino Acyl-tRNA Synthetases / Isoleucine-tRNA Ligase Language: En Journal: Nat Commun Year: 2022 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Amino Acyl-tRNA Synthetases / Isoleucine-tRNA Ligase Language: En Journal: Nat Commun Year: 2022 Document type: Article