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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40

  • Jang, Jinhwa (College of Pharmacy, Chungbuk National University) ;
  • Lee, Sung-Hee (College of Pharmacy, Chungbuk National University) ;
  • Kang, Dong-Hoon (College of Pharmacy, Chungbuk National University) ;
  • Sim, Dae-Won (Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University) ;
  • Ryu, Kyung-Suk (Research Center for Bioconvergence Analysis, Korea Basic Science Institute) ;
  • Jo, Ku-Sung (Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University) ;
  • Lee, Jinhyuk (Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Ryu, Hyojung (Korean Genomics Center (KOGIC), Ulsan National Institute of Science and Technology (UNIST)) ;
  • Kim, Eun-Hee (Research Center for Bioconvergence Analysis, Korea Basic Science Institute) ;
  • Won, Hyung-Sik (Department of Biotechnology, Research Institute (RIBHS) and College of Biomedical and Health Science, Konkuk University) ;
  • Kim, Ji-Hun (College of Pharmacy, Chungbuk National University)
  • Received : 2022.03.18
  • Accepted : 2022.05.18
  • Published : 2022.10.31
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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/phenylalanine-rich 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

Acknowledgement

This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2017R1A5A 2015541, 2019R1F1A1057427 and 2019R1A2C1004883) and by "Regional Inovation Strategy (RIS)" through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (MOE) (2021RIS-001). The use of NMR was supported by the Korea Basic Science Institute under the R&D program (Project No. C140440), supervised by the Ministry of Science and ICT.

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