Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
The specific pair of heat shock protein 70 (Hsp70) and Hsp40constitutes an essential molecular chaperone system involvedin numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members arecharacterized by the presence of a conserved J-domain (JD) thatfunctions as a co-chaperone of Hsp70. Tumorous imaginal disc1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3subfamily of Hsp40 and functions as a co-chaperone of themitochondrial Hsp70, mortalin. In this work, we performed nuclearmagnetic resonance spectroscopy to determine the solutionstructure of JD and its interaction with the glycine/phenylalaninerichregion (GF-motif) of human Tid1. Notably, Tid1-JD, whoseconformation was consistent with that of the DNAJB1 JD, appearedto stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present resultsdemonstrate that the functional and regulatory mode of Tid1resembles that of the DNAJB1 subfamily members rather thanDNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggestedthat an allosteric interaction between mortalin and Tid1is involved in the mitochondrial Hsp70/Hsp40 chaperone system.
Abstract
The specific pair of heat shock protein 70 (Hsp70) and Hsp40constitutes an essential molecular chaperone system involvedin numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members arecharacterized by the presence of a conserved J-domain (JD) thatfunctions as a co-chaperone of Hsp70. Tumorous imaginal disc1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3subfamily of Hsp40 and functions as a co-chaperone of themitochondrial Hsp70, mortalin. In this work, we performed nuclearmagnetic resonance spectroscopy to determine the solutionstructure of JD and its interaction with the glycine/phenylalaninerichregion (GF-motif) of human Tid1. Notably, Tid1-JD, whoseconformation was consistent with that of the DNAJB1 JD, appearedto stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present resultsdemonstrate that the functional and regulatory mode of Tid1resembles that of the DNAJB1 subfamily members rather thanDNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggestedthat an allosteric interaction between mortalin and Tid1is involved in the mitochondrial Hsp70/Hsp40 chaperone system.
참고문헌 (31)
- Jo KS, "Unique unfoldase", aggregase activity of a molecular chaperone Hsp33 in its holding-inactive state, 2019, pp.431, 1468~1480
- Keum M, "Molecular effects of elongation factor Ts and trigger factor on the unfolding and aggregation of elongation factor Tu induced by the prokaryotic molecular chaperone Hsp33", Biology(Basel), 10, pp.1171~ (2021)
- Mi-jee Kim, "Hepatitis B virus X protein enhances liver cancer cell migration by regulating calmodulin-associated actin polymerization", BMB Reports, 54(12), pp.614~619 (2021), 생화학분자생물학회
- Yochem J, "Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication", Mol Gen Genet, 164, pp.9~14 (1978)
- Kampinga HH, "The HSP70 chaperone machinery : J proteins as drivers of functional specificity", Nat Rev Mol Cell Biol, 11, pp.579~592 (2010)
- Mayer MP, "Hsp70 chaperones : cellular functions and molecular mechanism", Cell Mol Life Sci, 62, pp.670~684 (2005)
- Rosenzweig R, "The Hsp70 chaperone network", Nat Rev Mol Cell Biol, 20, pp.665~680 (2019)
- Cheetham ME, "Structure, function and evolution of DnaJ : conservation and adaptation of chaperone function", Cell stress & chaperones, 3, pp.28~36 (1998)
- Craig EA, "How do J-proteins get Hsp70 to do so many different things?", Trends Biochem Sci, 42, pp.355~368 (2017)
- Cyr DM, "DnaJ-like proteins : molecular chaperones and specific regulators of Hsp70", Trends Biochem Sci, 19, pp.176~181 (1994)
- Kelley WL, "The J-domain family and the recruitment of chaperone power", Trends Biochem Sci, 23, pp.222~227 (1998)
- Perrody E, "A bacteriophage-encoded J-domain protein interacts with the DnaK", Hsp70 chaperone and stabilizes the heat-shock factor sigma32 of Escherichia coli, 2012, pp.8, e1003037~
- Ahn BY, "Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer", Oncogene, 29, pp.1155~1166 (2010)
- Proft J, "Identification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson’s disease", PloS one, 6, pp.e26045~ (2011)
- Trinh DL, "Direct interaction between p53 and Tid1 proteins affects p53 mitochondrial localization and apoptosis", Oncotarget, 1, pp.396~404 (2010)
- Zhou C, "Beta-Amyloid increases the expression levels of Tid1 responsible for neuronal cell death and amyloid beta production", Mol Neurobiol, 57, pp.1099~1114 (2020)
- Wang SF, "DNAJA3", Tid1 is required for mitochondrial dna maintenance and regulates migration and invasion of human gastric cancer cells, 2020, pp.12, 3463~
- Syken J, "TID1, a human homolog of the Drosophila tumor suppressor l(2)tid, encodes two mitochondrial modulators of apoptosis with opposing functions", Proc Natl Acad Sci, 96, pp.8499~8504 (1999)
- Faust O, "HSP40 proteins use class-specific regulation to drive HSP70functional diversity", Nature, 587, pp.489~494 (2020)
- 조구성, "Backbone NMR Assignments of a Putative p53-binding Domain of the Mitochondrial Hsp40, Tid1", Journal of the Korean Magnetic Resonance Society, 22(3), pp.64~70 (2018), 한국자기공명학회[DOI]
- Kay LE, "Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy : application to staphylococcal nuclease", Biochemistry, 28, pp.8972~8979 (1989)
- Kneller JM, "An effective method for the discrimination of motional anisotropy and chemical exchange", J Am Chem Soc, 124, pp.1852~1853 (2002)
- Delaglio F, "NMRPipe : a multidimensional spectral processing system based on UNIX pipes", J Biomol NMR, 6, pp.277~293 (1995)
- Johnson BA, "Using NMRView to visualize and analyze the NMR spectra of macromolecules", Methods Mol Biol, 278, pp.313~352 (2004)
- Guntert P, "Automated NMR structure calculation with CYANA", Methods Mol Biol, 278, pp.353~378 (2004)
- Shen Y, "TALOS+ : a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts", J Biomol NMR, 44, pp.213~223 (2009)
- Kim TR, "Statistical torsion angle potential energy functions for protein structure modeling : a bicubic interpolation approach", Proteins, 81, pp.1156~1165 (2013)
- Brooks BR, "CHARMM : the biomolecular simulation program", J Comput Chem, 30, pp.1545~1614 (2009)
- Shen MY, "Statistical potential for assessment and prediction of protein structures", Protein Sci, 15, pp.2507~2524 (2006)
- Zhou H, "Protein structure prediction by pro-Sp3-TASSER", Biophys J, 96, pp.2119~2127 (2009)
- Williams CJ, "MolProbity : more and better reference data for improved all-atom structure validation", Protein Sci, 27, pp.293~315 (2018)