Overproduction and biophysical characterization of human HSP70 proteins

Protein Expression and Purification

Volumn 106, Issue , 2015, Pages 57-65

  Boswell Casteel, Rebba C ^a   Johnson, Jennifer M ^a   Duggan, Kelli D ^a   Tsutsui, Yuko ^a   Hays, Franklin A ^a,b  

^a UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF OKLAHOMA HEALTH SCIENCES CENTER   (United States)

Author keywords

Enzyme purification; Heat shock protein; HSP70; Molecular chaperone; Recombinant protein expression

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70;

BIOCHEMISTRY; BIOPHYSICS; CIRCULAR DICHROISM; HUMAN; HYDROLYSIS; ISOLATION AND PURIFICATION; KINETICS; LIGHT; METABOLISM; PROCEDURES; PROTEIN DENATURATION; PROTEIN UNFOLDING; RADIATION SCATTERING; TEMPERATURE; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATASES; BIOCHEMISTRY; BIOPHYSICAL PHENOMENA; CIRCULAR DICHROISM; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; KINETICS; LIGHT; PROTEIN DENATURATION; PROTEIN UNFOLDING; SCATTERING, RADIATION; TEMPERATURE; ULTRACENTRIFUGATION;

EID: 84911928273     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2014.09.013     Document Type: Article

References (61)

1. D. Athanasiou, M. Kosmaoglou, N. Kanuga, S.S. Novoselov, A.W. Paton, J.C. Paton, J.P. Chapple, and M.E. Cheetham BiP prevents rod opsin aggregation Mol. Biol. Cell 23 2012 3522 3531
2. I.J. Benjamin, and D.R. McMillan Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease Circ. Res. 83 1998 117 132
3. R.S. Gupta, and B. Singh Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus Curr. Biol. 4 1994 1104 1114
4. S. Lindquist, and E.A. Craig The heat-shock proteins Annu. Rev. Genet. 22 1988 631 677
5. H.R. Pelham Hsp70 accelerates the recovery of nucleolar morphology after heat shock EMBO J. 3 1984 3095 3100
6. G.C. Li, L.G. Li, Y.K. Liu, J.Y. Mak, L.L. Chen, and W.M. Lee Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene Proc. Natl. Acad. Sci. U.S.A. 88 1991 1681 1685
7. N.B. Radford, M. Fina, I.J. Benjamin, R.W. Moreadith, K.H. Graves, P. Zhao, S. Gavva, A. Wiethoff, A.D. Sherry, C.R. Malloy, and R.S. Williams Cardioprotective effects of 70-kDa heat shock protein in transgenic mice Proc. Natl. Acad. Sci. U.S.A. 93 1996 2339 2342
8. M. Daugaard, M. Rohde, and M. Jaattela The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions FEBS Lett. 581 2007 3702 3710
9. H.H. Kampinga, J. Hageman, M.J. Vos, H. Kubota, R.M. Tanguay, E.A. Bruford, M.E. Cheetham, B. Chen, and L.E. Hightower Guidelines for the nomenclature of the human heat shock proteins Cell Stress Chaperones 14 2009 105 111
10. T. Gidalevitz, F. Stevens, and Y. Argon Orchestration of secretory protein folding by ER chaperones Biochim. Biophys. Acta 1833 2013 2410 2424
11. M. Wang, S. Wey, Y. Zhang, R. Ye, and A.S. Lee Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders Antioxid. Redox Signal. 11 2009 2307 2316
12. H. Coe, and M. Michalak Calcium binding chaperones of the endoplasmic reticulum Gen. Physiol. Biophys. 28 Spec No Focus 2009 F96 F103
13. C. Hetz The unfolded protein response: controlling cell fate decisions under ER stress and beyond Nat. Rev. Mol. Cell Biol. 13 2012 89 102
14. H.P. Harding, and D. Ron Endoplasmic reticulum stress and the development of diabetes: a review Diabetes 51 Suppl. 3 2002 S455 S461
15. L. Zhao, C. Longo-Guess, B.S. Harris, J.W. Lee, and S.L. Ackerman Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP Nat. Genet. 37 2005 974 979
16. D. Dong, M. Ni, J. Li, S. Xiong, W. Ye, J.J. Virrey, C. Mao, R. Ye, M. Wang, L. Pen, L. Dubeau, S. Groshen, F.M. Hofman, and A.S. Lee Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development Cancer Res. 68 2008 498 505
17. J. Li, and A.S. Lee Stress induction of GRP78/BiP and its role in cancer Curr. Mol. Med. 6 2006 45 54
18. A.C. Ranganathan, L. Zhang, A.P. Adam, and J.A. Aguirre-Ghiso Functional coupling of p38-induced up-regulation of BiP and activation of RNA-dependent protein kinase-like endoplasmic reticulum kinase to drug resistance of dormant carcinoma cells Cancer Res. 66 2006 1702 1711
19. R.K. Reddy, C. Mao, P. Baumeister, R.C. Austin, R.J. Kaufman, and A.S. Lee Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation J. Biol. Chem. 278 2003 20915 20924
20. T.G. Chappell, W.J. Welch, D.M. Schlossman, K.B. Palter, M.J. Schlesinger, and J.E. Rothman Uncoating ATPase is a member of the 70 kilodalton family of stress proteins Cell 45 1986 3 13
21. S.B. Goldfarb, O.B. Kashlan, J.N. Watkins, L. Suaud, W. Yan, T.R. Kleyman, and R.C. Rubenstein Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels Proc. Natl. Acad. Sci. U.S.A. 103 2006 5817 5822
22. A. Ziemienowicz, M. Zylicz, C. Floth, and U. Hubscher Calf thymus Hsc70 protein protects and reactivates prokaryotic and eukaryotic enzymes J. Biol. Chem. 270 1995 15479 15484
23. W.J. Chirico, M.G. Waters, and G. Blobel 70 K heat shock related proteins stimulate protein translocation into microsomes Nature 332 1988 805 810
24. P.J. Hollenbeck, and W.M. Saxton The axonal transport of mitochondria J. Cell Sci. 118 2005 5411 5419
25. K. Hirasaka, K. Tokuoka, R. Nakao, C. Yamada, M. Oarada, T. Imagawa, K. Ishidoh, Y. Okumura, K. Kishi, and T. Nikawa Cathepsin C propeptide interacts with intestinal alkaline phosphatase and heat shock cognate protein 70 in human Caco-2 cells J. Physiol. Sci. 58 2008 105 111
26. K. Tanaka, T. Namba, Y. Arai, M. Fujimoto, H. Adachi, G. Sobue, K. Takeuchi, A. Nakai, and T. Mizushima Genetic evidence for a protective role for heat shock factor 1 and heat shock protein 70 against colitis J. Biol. Chem. 282 2007 23240 23252
27. F.F. Yan, E.B. Pratt, P.C. Chen, F. Wang, W.R. Skach, L.L. David, and S.L. Shyng Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex Mol. Biol. Cell 21 2010 1945 1954
28. L. Florin, K.A. Becker, C. Sapp, C. Lambert, H. Sirma, M. Muller, R.E. Streeck, and M. Sapp Nuclear translocation of papillomavirus minor capsid protein L2 requires Hsc70 J. Virol. 78 2004 5546 5553
29. T. Liu, C.K. Daniels, and S. Cao Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential Pharmacol. Ther. 136 2012 354 374
30. R. Wadhwa, S.C. Kaul, Y. Ikawa, and Y. Sugimoto Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype J. Biol. Chem. 268 1993 6615 6621
31. R. Wadhwa, S.C. Kaul, Y. Mitsui, and Y. Sugimoto Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts Exp. Cell. Res. 207 1993 442 448
32. R. Wadhwa, S. Takano, M. Robert, A. Yoshida, H. Nomura, R.R. Reddel, Y. Mitsui, and S.C. Kaul Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member J. Biol. Chem. 273 1998 29586 29591
33. S.C. Kaul, C.C. Deocaris, and R. Wadhwa Three faces of mortalin: a housekeeper, guardian and killer Exp. Gerontol. 42 2007 263 274
34. M.P. Mayer, and B. Bukau Hsp70 chaperones: cellular functions and molecular mechanism Cell. Mol. Life Sci. 62 2005 670 684
35. Y.W. Chang, Y.J. Sun, C. Wang, and C.D. Hsiao Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation J. Biol. Chem. 283 2008 15502 15511
36. C.J. Harrison, M. Hayer-Hartl, M. Di Liberto, F. Hartl, and J. Kuriyan Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK Science 276 1997 431 435
37. M. Wisniewska, T. Karlberg, L. Lehtio, I. Johansson, T. Kotenyova, M. Moche, and H. Schuler Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78 PLoS ONE 5 2010 e8625
38. K.M. Flaherty, C. DeLuca-Flaherty, and D.B. McKay Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein Nature 346 1990 623 628
39. J. Amick, S.E. Schlanger, C. Wachnowsky, M.A. Moseng, C.C. Emerson, M. Dare, W.I. Luo, S.S. Ithychanda, J.C. Nix, J.A. Cowan, R.C. Page, and S. Misra Crystal structure of the nucleotide-binding domain of mortalin, the mitochondrial Hsp70 chaperone Protein Sci. 23 2014 833 842
40. A.T. Macias, D.S. Williamson, N. Allen, J. Borgognoni, A. Clay, Z. Daniels, P. Dokurno, M.J. Drysdale, G.L. Francis, C.J. Graham, R. Howes, N. Matassova, J.B. Murray, R. Parsons, T. Shaw, A.E. Surgenor, L. Terry, Y. Wang, M. Wood, and A.J. Massey Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity J. Med. Chem. 54 2011 4034 4041
41. J.F. Swain, G. Dinler, R. Sivendran, D.L. Montgomery, M. Stotz, and L.M. Gierasch Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker Mol. Cell 26 2007 27 39
42. J. Jiang, K. Prasad, E.M. Lafer, and R. Sousa Structural basis of interdomain communication in the Hsc70 chaperone Mol. Cell 20 2005 513 524
43. M. Vogel, M.P. Mayer, and B. Bukau Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker J. Biol. Chem. 281 2006 38705 38711
44. H. Wang, A.V. Kurochkin, Y. Pang, W. Hu, G.C. Flynn, and E.R. Zuiderweg NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction Biochemistry 37 1998 7929 7940
45. M. Vogel, B. Bukau, and M.P. Mayer Allosteric regulation of Hsp70 chaperones by a proline switch Mol. Cell 21 2006 359 367
46. R. Jordan, and R. McMacken Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins J. Biol. Chem. 270 1995 4563 4569
47. M. Li, F.A. Hays, Z. Roe-Zurz, L. Vuong, L. Kelly, C.M. Ho, R.M. Robbins, U. Pieper, J.D. O'Connell 3rd, L.J. Miercke, K.M. Giacomini, A. Sali, and R.M. Stroud Selecting optimum eukaryotic integral membrane proteins for structure determination by rapid expression and solubilization screening J. Mol. Biol. 385 2009 820 830
48. F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expr. Purif. 41 2005 207 234
49. B. Demeler, G. Gorbet, D. Zollars, B. Dubbs, E. Brookes, and W. Cao Ultrascan-III Version 2.2: A Comprehensive Data Analysis Software Package for Analytical Ultracentrifugation Experiments 2014
50. B. Demeler Methods for the design and analysis of sedimentation velocity and sedimentation equilibrium experiments with proteins Curr. Protoc. Protein Sci. 60:7.13 2010 7.13.1 7.13.24
51. B. Demeler, and K.E. van Holde Sedimentation velocity analysis of highly heterogeneous systems Anal. Biochem. 335 2004 279 288
52. W.I. Luo, E. Dizin, T. Yoon, and J.A. Cowan Kinetic and structural characterization of human mortalin Protein Expr. Purif. 72 2010 75 81
53. T. Arakawa, and K. Tsumoto The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation Biochem. Biophys. Res. Commun. 304 2003 148 152
54. S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310
55. M. Yasuda, Y. Murakami, A. Sowa, H. Ogino, and H. Ishikawa Effect of additives on refolding of a denatured protein Biotechnol. Prog. 14 1998 601 606
56. A. Tischer, H. Lilie, R. Rudolph, and C. Lange l-arginine hydrochloride increases the solubility of folded and unfolded recombinant plasminogen activator rPA Protein Sci. 19 2010 1783 1795
57. A. Zarrine-Afsar, A. Mittermaier, L.E. Kay, and A.R. Davidson Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain Protein Sci. 15 2006 162 170
58. Y.D. Clonis, N.E. Labrou, V.P. Kotsira, C. Mazitsos, S. Melissis, and G. Gogolas Biomimetic dyes as affinity chromatography tools in enzyme purification J. Chromatogr. A 891 2000 33 44
59. S.T. Thompson, K.H. Cass, and E. Stellwagen Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins Proc. Natl. Acad. Sci. U.S.A. 72 1975 669 672
60. S.T. Thompson, and E. Stellwagen Binding of Cibacron blue F3GA to proteins containing the dinucleotide fold Proc. Natl. Acad. Sci. U.S.A. 73 1976 361 365
61. S.T. Thompson, R. Cass, and E. Stellwagen A quantitative procedure for recovery of nucleoside phosphate ligands and preparation of apoprotein from holoproteins using blue dextran-Sepharose chromatography Anal. Biochem. 72 1976 293 296