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Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40
Jinhwa Jang 1,# (Graduate student), Sung-Hee Lee 1,# (Graduate student), Dong-Hoon Kang 1 (Graduate student), Dae-Won Sim 2 (Post Doctor), Kyung-Suk Ryu 3 (Professor), Ku-Sung Jo 2 (Graduate student), Jinhyuk Lee 4,5 (Professor), Hyojung Ryu 6,7 (Graduate student), Eun-Hee Kim 3 (Researcher), Hyung-Sik Won 2,8,# (Professor), Ji-Hun Kim 1,*,# (Professor)
1College of Pharmacy, Chungbuk National University,
2Department of Biotechnology, College of Biomedical and Health Science, Konkuk University,
3Research Center for Bioconvergence Analysis, Korea Basic Science Institute,
4Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB),
5Department of Bioinformatics, KRIBB School of Bioscience, University of Science and Technology (UST),
6Korean Genomics Center (KOGIC), Ulsan National Institute of Science and Technology (UNIST),
7Department of Biomedical Engineering, College of Information and Biotechnology, UNIST,
8BK21 Project Team, Department of Applied Life Science, Graduate School, Konkuk University
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.
Abstract, Accepted Manuscript(in press) [Submitted on March 18, 2022, Accepted on May 18, 2022]
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