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

Author

Listed:
  • 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
    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)
    Ulsan National Institute of Science and Technology)

  • Yunje Cho

    (Pohang University of Science and Technology)

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.

Suggested Citation

  • 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 & , 2022. "Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34612-y
    DOI: 10.1038/s41467-022-34612-y
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