BMB Reports 2022; 55(10): 488-493  https://doi.org/10.5483/BMBRep.2022.55.10.051
Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40
Jinhwa Jang1,# , Sung-Hee Lee1,# , Dong-Hoon Kang1 , Dae-Won Sim2 , Kyung-Suk Ryu3 , Ku-Sung Jo2 , Jinhyuk Lee4,5 , Hyojung Ryu6,7 , Eun-Hee Kim3 , Hyung-Sik Won2,8,* & Ji-Hun Kim1,*
1College of Pharmacy, Chungbuk National University, Cheongju 28160, 2Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University, Chungju 27478, 3Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Cheongju 28119, 4Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, 5Department of Bioinformatics, KRIBB School of Bioscience, University of Science and Technology (UST), Daejeon 34113, 6Korean Genomics Center (KOGIC), Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, 7Department of Biomedical Engineering, College of Information and Biotechnology, UNIST, Ulsan 44919, 8BK21 Project Team, Department of Applied Life Science, Graduate School, Konkuk University, Chungju 27478, Korea
Correspondence to: Ji-Hun Kim, Tel: +82-43-249-1343; Fax: +82-43-268-2732; E-mail: nmrjhkim@cbnu.ac.kr; Hyung-Sik Won, Tel: +82-43-840-3589; Fax: +82-43-840-3048; E-mail: wonhs@kku.ac.kr
#These authors contributed equally to this work.
Received: March 18, 2022; Revised: April 11, 2022; Accepted: May 18, 2022; Published online: October 31, 2022.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

cc This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
ABSTRACT
The specific pair of heat shock protein 70 (Hsp70) and Hsp40 constitutes an essential molecular chaperone system involved in numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members are characterized by the presence of a conserved J-domain (JD) that functions as a co-chaperone of Hsp70. Tumorous imaginal disc 1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3 subfamily of Hsp40 and functions as a co-chaperone of the mitochondrial Hsp70, mortalin. In this work, we performed nuclear magnetic resonance spectroscopy to determine the solution structure of JD and its interaction with the glycine/phenylalaninerich region (GF-motif) of human Tid1. Notably, Tid1-JD, whose conformation was consistent with that of the DNAJB1 JD, appeared to stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present results demonstrate that the functional and regulatory mode of Tid1 resembles that of the DNAJB1 subfamily members rather than DNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggested that an allosteric interaction between mortalin and Tid1 is involved in the mitochondrial Hsp70/Hsp40 chaperone system.
Keywords: DNAJ family, GF-motif, Hsp40, Hsp70, J-domain, Nuclear magnetic resonance (NMR), Tid1

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Funding Information
  • National Research Foundation of Korea
      10.13039/501100003725
      NRF-2017R1A5A2015541, 2019R1F1A1057427, 2019R1A2C1004883, 2021RIS-001
  • Ministry of Education
      10.13039/501100002701
      NRF-2017R1A5A2015541, 2019R1F1A1057427, 2019R1A2C1004883, 2021RIS-001
  • Korea Basic Science Institute
      10.13039/501100003716
      C140440

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