Heat-shock response transcriptional program enables high-yield and high-quality recombinant protein production in Escherichia coli

ACS Chemical Biology

Volumn 9, Issue 9, 2014, Pages 1945-1949

  Zhang, Xin ^a   Liu, Yu ^a   Genereux, Joseph C ^a   Nolan, Chandler ^a   Singh, Meha ^a   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR; ARABINOSE; CHAPERONIN 60; DNAJ PROTEIN, E COLI; EARLY PREGNANCY FACTOR; ESCHERICHIA COLI PROTEIN; GRPE PROTEIN, E COLI; HEAT SHOCK PROTEIN 40; HEAT-SHOCK SIGMA FACTOR 32; SIGMA FACTOR;

ANIMAL CELL; ARTICLE; BACTERIAL GROWTH; BIOSYNTHESIS; ENERGY YIELD; ESCHERICHIA COLI; HEAT SHOCK RESPONSE; HUMAN; NEGATIVE FEEDBACK; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN HOMEOSTASIS; STOICHIOMETRY; ANTIBIOTIC RESISTANCE; FEEDBACK SYSTEM; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; MUTATION; PROCEDURES; PROTEIN ENGINEERING; PROTEOMICS; TEMPERATURE;

ESCHERICHIA COLI;

ARABINOSE; CHAPERONIN 10; CHAPERONIN 60; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FEEDBACK, PHYSIOLOGICAL; GENE EXPRESSION REGULATION, BACTERIAL; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HSP40 HEAT-SHOCK PROTEINS; KANAMYCIN RESISTANCE; MUTATION; PROTEIN ENGINEERING; PROTEOMICS; RECOMBINANT PROTEINS; SIGMA FACTOR; TEMPERATURE; TRANSCRIPTION, GENETIC;

EID: 84912562059     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb5004477     Document Type: Article

References (34)

1. Baneyx, F., and Mujacic, M. (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22, 1399-1408.
2. Thomas, J. G., Ayling, A., and Baneyx, F. (1997) Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli - To fold or to refold. Appl. Biochem. Biotechnol. 66, 197-238.
3. de Marco, A. (2011) Molecular and chemical chaperones for improving the yields of soluble recombinant proteins. Methods Mol. Biol. 705, 31-51.
4. Bukau, B., Deuerling, E., Pfund, C., and Craig, E. A. (2000) Getting newly synthesized proteins into shape. Cell 101, 119-122.
5. Hartl, F. U., and Hayer-Hartl, M. (2009) Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574-581.
6. Horwich, A. L., Fenton, W. A., Chapman, E., and Farr, G. W. (2007) Two families of chaperonin: physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23, 115-145.
7. Mamathambika, B. S., and Bardwell, J. C. (2008) Disulfide-linked protein folding pathways. Annu. Rev. Cell Dev. Biol. 24, 211-235.
8. Thomas, J. G., and Baneyx, F. (1996) Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing Heat-shock proteins. J. Biol. Chem. 271, 11141-11147.
9. Baneyx, F., and Palumbo, J. L. (2003) Improving heterologous protein folding via molecular chaperone and foldase co-expression. Methods Mol. Biol. 205, 171-197.
10. de Marco, A., and De Marco, V. (2004) Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J. Biotechnol. 109, 45-52.
11. de Marco, A. (2007) Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat. Protoc. 2, 2632-2639.
12. Rudiger, S., Germeroth, L., SchneiderMergener, J., and Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507.
13. Houry, W. A., Frishman, D., Eckerskorn, C., Lottspeich, F., and Hartl, F. U. (1999) Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147-154.
14. Lindquist, S. (1986) The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191.
15. Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008) Adapting proteostasis for disease intervention. Science 319, 916-919.
16. Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., and Balch, W. E. (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78, 959-991.
17. Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
18. Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M., and Hartl, F. U. (2013) Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82, 323-355.
19. Straus, D. B., Walter, W. A., and Gross, C. A. (1987) The heat-shock response of Escherichia coli is regulated by changes in the concentration of σ-32. Nature 329, 348-351.
20. Zhao, K., Liu, M. Z., and Burgess, R. R. (2005) The global transcriptional response of Escherichia coli to induced σ(32) protein involves σ(32) regulon activation followed by inactivation and degradation of σ(32) in vivo. J. Biol. Chem. 280, 17758-17768.
21. Valdez-Cruz, N. A., Caspeta, L., Perez, N. O., Ramirez, O. T., and Trujillo-Roldan, M. A. (2010) Production of recombinant proteins in E. coli by the heat inducible expression system based on the phage lambda pL and/or pR promoters. Microb. Cell Fact. 9, 18.
22. Wu, H., Pei, J., Jiang, Y., Song, X., and Shao, W. (2010) pHsh vectors, a novel expression system of Escherichia coli for the large-scale production of recombinant enzymes. Biotechnol. Lett. 32, 795-801.
23. Hsu, S. Y., Lin, Y. S., Li, S. J., and Lee, W. C. (2014) Co-expression of a heat shock transcription factor to improve conformational quality of recombinant protein in Escherichia coli. J. Biosci. Bioeng., DOI: 10.1016/j.jbiosc.2014.1002.1012.
24. Guisbert, E., Herman, C., Lu, C. Z., and Gross, C. A. (2004) A chaperone network controls the heat shock response in E. coli. Genes Dev. 18, 2812-2821.
25. Yura, T., Guisbert, E., Poritz, M., Lu, C. Z., Campbell, E., and Gross, C. A. (2007) Analysis of σ(32) mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response. Proc. Natl. Acad. Sci. U.S.A. 104, 17638-17643.
26. Bukau, B., Weissman, J., and Horwich, A. (2006) Molecular chaperones and protein quality control. Cell 125, 443-451.
27. Bjelic, S., Kipnis, Y., Wang, L., Pianowski, Z., Vorobiev, S., Su, M., Seetharaman, J., Xiao, R., Kornhaber, G., Hunt, J. F., Tong, L., Hilvert, D., and Baker, D. (2014) Exploration of alternate catalytic mechanisms and optimization strategies for retroaldolase design. J. Mol. Biol. 426, 256-271.
28. Liu, Y., Tan, Y. L., Zhang, X., Bhabha, G., Ekiert, D. C., Genereux, J. C., Cho, Y., Kipnis, Y., Bjelic, S., Baker, D., and Kelly, J. W. (2014) Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts. Proc. Natl. Acad. Sci. U.S.A. 111, 4449-4454.
29. Xue, Y., Wu, A., Zeng, H., and Shao, W. (2006) High-level expression of an α-L-arabinofuranosidase from Thermotoga maritima in Escherichia coli for the production of xylobiose from xylan. Biotechnol. Lett. 28, 351-356.
30. Calamini, B., Silva, M. C., Madoux, F., Hutt, D. M., Khanna, S., Chalfant, M. A., Saldanha, S. A., Hodder, P., Tait, B. D., Garza, D., Balch, W. E., and Morimoto, R. I. (2012) Small-molecule proteostasis regulators for protein conformational diseases. Nat. Chem. Biol. 8, 185-196.
31. Shoulders, M. D., Ryno, L. M., Cooley, C. B., Kelly, J. W., and Wiseman, R. L. (2013) Broadly applicable methodology for the rapid and dosable small molecule-mediated regulation of transcription factors in human cells. J. Am. Chem. Soc. 135, 8129-8132.
32. Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., Yates, J. R., 3rd, Su, A. I., Kelly, J. W., and Wiseman, R. L. (2013) Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep. 3, 1279-1292.
33. Wang, A. M., Miyata, Y., Klinedinst, S., Peng, H. M., Chua, J. P., Komiyama, T., Li, X., Morishima, Y., Merry, D. E., Pratt, W. B., Osawa, Y., Collins, C. A., Gestwicki, J. E., and Lieberman, A. P. (2013) Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation. Nat. Chem. Biol. 9, 112-118.
34. Ryno, L. M., Genereux, J. C., Naito, T., Morimoto, R. I., Powers, E. T., Shoulders, M. D., and Wiseman, R. L. (2014) Characterizing the altered cellular proteome induced by the stress-independent activation of Heat Shock Factor 1. ACS Chem. Biol. 9, 1273-1283.