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) |
1 | Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278, 313-352 |
2 | Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278, 353-378 |
3 | Kim TR, Yang JS, Shin S and Lee J (2013) Statistical torsion angle potential energy functions for protein structure modeling: a bicubic interpolation approach. Proteins 81, 1156-1165 DOI |
4 | Zhou H and Skolnick J (2009) Protein structure prediction by pro-Sp3-TASSER. Biophys J 96, 2119-2127 DOI |
5 | Keum M, Ito D, Kim MS et al (2021) 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, 1171 |
6 | Yochem J, Uchida H, Sunshine M, Saito H, Georgopoulos CP and Feiss M (1978) Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol Gen Genet 164, 9-14 DOI |
7 | Kampinga HH and Craig EA (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11, 579-592 DOI |
8 | Rosenzweig R, Nillegoda NB, Mayer MP and Bukau B (2019) The Hsp70 chaperone network. Nat Rev Mol Cell Biol 20, 665-680 DOI |
9 | Cyr DM, Langer T and Douglas MG (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19, 176-181 DOI |
10 | Ahn BY, Trinh DL, Zajchowski LD, Lee B, Elwi AN and Kim SW (2010) Tid1 is a new regulator of p53 mitochondrial translocation and apoptosis in cancer. Oncogene 29, 1155-1166 DOI |
11 | Brooks BR, Brooks CL 3rd, Mackerell AD Jr et al (2009) CHARMM: the biomolecular simulation program. J Comput Chem 30, 1545-1614 DOI |
12 | Williams CJ, Headd JJ, Moriarty NW et al (2018) MolProbity: more and better reference data for improved all-atom structure validation. Protein Sci 27, 293-315 DOI |
13 | Cheetham ME and Caplan AJ (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell stress & chaperones 3, 28-36 DOI |
14 | Kelley WL (1998) The J-domain family and the recruitment of chaperone power. Trends Biochem Sci 23, 222-227 DOI |
15 | Shen Y, Delaglio F, Cornilescu G and Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44, 213-223 DOI |
16 | Shen MY and Sali A (2006) Statistical potential for assessment and prediction of protein structures. Protein Sci 15, 2507-2524 DOI |
17 | Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J and Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6, 277-293 |
18 | Jo KS, Kim JH, Ryu KS et al (2019) Unique unfoldase/aggregase activity of a molecular chaperone Hsp33 in its holding-inactive state. J Mol Biol 431, 1468-1480 DOI |
19 | Kim MJ, Kim J, Im JS, Kang I and Ahn JK (2021) Hepatitis B virus X protein enhances liver cancer cell migration by regulating calmodulin-associated actin polymerization. BMB Rep 54, 614-619 DOI |
20 | Perrody E, Cirinesi AM, Desplats C et al (2012) A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor sigma32 of Escherichia coli. PLoS Genet 8, e1003037 DOI |
21 | Proft J, Faraji J, Robbins JC et al (2011) Identification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson's disease. PloS one 6, e26045 DOI |
22 | Mayer MP and Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62, 670-684 DOI |
23 | Craig EA and Marszalek J (2017) How do J-proteins get Hsp70 to do so many different things? Trends Biochem Sci 42, 355-368 DOI |
24 | Trinh DL, Elwi AN and Kim SW (2010) Direct interaction between p53 and Tid1 proteins affects p53 mitochondrial localization and apoptosis. Oncotarget 1, 396-404 DOI |
25 | Zhou C, Taslima F, Abdelhamid M et al (2020) Beta-Amyloid increases the expression levels of Tid1 responsible for neuronal cell death and amyloid beta production. Mol Neurobiol 57, 1099-1114 DOI |
26 | Wang SF, Huang KH, Tseng WC et al (2020) DNAJA3/Tid1 is required for mitochondrial dna maintenance and regulates migration and invasion of human gastric cancer cells. Cancers (Basel) 12, 3463 DOI |
27 | Syken J, De-Medina T and Munger K (1999) 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, 8499-8504 DOI |
28 | Faust O, Abayev-Avraham M, Wentink AS et al (2020) HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. Nature 587, 489-494 DOI |
29 | Jo KS, Sim DW, Kim EH et al (2018) Backbone NMR assignments of a putative p53-binding domain of the mitochondrial Hsp40, Tid1. J Kor Magn Reson Soc 22, 64-70 |
30 | Kay LE, Torchia DA and Bax A (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979 DOI |
31 | Kneller JM, Lu M and Bracken C (2002) An effective method for the discrimination of motional anisotropy and chemical exchange. J Am Chem Soc 124, 1852-1853 DOI |