Effect of molecular chaperones on the soluble expression of alginate lyase in E. coli

Biotechnology and Bioprocess Engineering

Volumn 11, Issue 5, 2006, Pages 414-419

  Shin, Eun Jung ^a   Park, So Lim ^b   Jeon, Sung Jong ^a   Lee, Jin Woo ^c   Kim, Young Tae ^d   Kim, Yeon Hee ^e   Nam, Soo Wan ^a  

^a Dong Eui University   (South Korea)

^b Bioleaders Corporation   (South Korea)

^c Dong A University   (South Korea)

^d Pukyong National University   (South Korea)

^e OSAKA UNIVERSITY   (Japan)

Author keywords

Alginate lyase; Coexpression; E. coli; Molecular chaperone

Indexed keywords

ALGINIC ACID; ARABINOSE; CHAPERONE; CHAPERONIN; LYASE; PROTEIN DNAJ; PROTEIN DNAK;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ESCHERICHIA COLI; FACILITATION; NONHUMAN; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN FOLDING; SOLUBILITY;

PSEUDOALTEROMONAS ELYAKOVII;

EID: 33750721301     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02932308     Document Type: Article

References (34)

1. Sawabe, T., H. Takahashi, Y. Ezura, and P. Gacesa (2001) Cloning, sequence analysis and expression of Pseudoalteromonas elyakovii IAM 14594 gene (alyPEEC) encoding the extracellular alginate lyase. Carbohydr. Res. 335: 11-21.
2. Preiss, J. and G. Ashwell (1962) Alginic acid metabolism in bacteria. J. Biol. Chem. 237: 309-316.
3. Yoon, H. J., W. Hashimoto, O. Miyake, M. Okamoto, B. Mikami, and K. Murata (2000) Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases. Protein Expr. Purif. 19: 84-90.
4. Onsøyen, E, (1996) Commercial applications of alginates. Carbohydr. Eur. 14: 26-31.
5. Renn, D. (1997) Biotechnology and the red seaweed polysaccharide industry: status, needs and prospects. Trends Biotechnol. 15: 9-14.
6. Murata, K, T. Inose, T. Hisano, S. Abe, Y. Yonemoto, T. Yamashita, M. Takagi, K. Sakaguchi, A. Kimura, and T. Imanaka (1993) Bacterial alginate lyase: enzymology, genetics and application. J. Ferment. Bioeng. 76: 427-437.
7. Kim, J. E., E. J. Kim, W. J. Rhee, and T. H. Park (2005) Enhanced production of recombinant protein in Escherichia coli using silkworm hemolymph. Biotechnol. Bioprocess Eng. 10: 353-356.
8. Jin, H. H., N. S. Han, D. K. Kweon, Y. C. Park, and J. H. Soo (2001) Effects of environmental factors on in vivo folding of Bacillus macerans cyclodextrin glycosyltransferase in recombinant Escherichia coli. J. Microbiol. Biotechnol, 11: 92-96.
9. Kim, C. I., M. D. Kim, Y. C. Park, N. S. Han, and J. H. Soo (2000) Refolding of Bacillus macerans cyclodextrin glucanotransferase expressed as inclusion bodies in recombinant Escherichia coli. J. Microbiol. Biotechnol. 10: 632-637.
10. Kondo, A., J. Kohda, Y. Endo, T. Shiromizu, Y. Kurokawa, K. Nishihara, H. Yanagi, T. Yura, and H. Fukuda (2000) Improvement of productivity of active horseradish peroxidase in Escherichia coli by coexpression of Dsb proteins. J. Biosci. Bioeng. 90: 600-606.
11. Thomas, J. G., A. Ayling, and F. Baneyx (1997) Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. Appl. Biochem. Biotechnol. 66: 197-238.
12. Kim, H. and I. H. Kim (2005) Refolding of fusion ferritin by gel filtration chromatography (GFC). Biotechnol. Bioprocess Eng. 10: 500-504.
13. Guan, Y.-X., H.-X. Pan, Y.-G. Gao, S.-J. Yao, and M.-G. Cho (2005) Refolding and purification of recombinant human interferon-γ expressed as inclusion bodies in Escherichia coli using size exclusion chromatography. Biotechnol. Bioprocess Eng. 10: 122-127.
14. Kwon, M. J., S. L. Park, S. K. Kim, and S. W. Nam (2002) Overproduction of Bacillus macerans cyclodextrin glucanotransferase in E. coli by coexpression of GroEL/ES chaperone. J. Microbiol. Biotechnol. 12: 1002-1005.
15. Lamark, T., M. Ingebrigtsen, C. Bjornstad, T. Melkko, T. E. Mollnes, and E. W. Nielsen (2001) Expression of active human C1 inhibitor serpin domain in Escherichia coli. Protein Expr. Purif. 22: 349-358.
16. Park, S. L., M. J. Kwon, S. K. Kim, and S. W. Nam (2004) GroEL/ES chaperone and low culture temperature synergistically enhanced the soluble expression of CGTase in E. coli. J. Microbiol. Biotechnol. 14: 216-219.
17. Sareen, D., R. Sharma, and R. M. Vohra (2001) Chaperone-assisted overexpression of an active D-carbamoylase from Agrobacterium tumefaciens AM 10. Protein Expr. Purif. 23: 374-379.
18. Hoshino, K, A. Eda, Y. Kurokawa, and N. Shimizu (2002) Production of brain-derived neurotrophic factor in Escherichia coli by coexpression. of Dsb proteins. Biosci. Biotechnol. Biochem. 66: 344-350.
19. Kurokawa, Y., H. Yanagi, and T. Yura (2000) Overexpression of protein disulfide isomerase DsbD stabilize multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli. Appl. Environ. Microbiol. 66: 3960-3965.
20. Han, M. J., S. J. Park, T. J. Park, and S. Y. Lee (2004) Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli. Biotechnol. Bioeng. 88: 426-436.
21. Chung, K. T., T. H. Lee, and G. S. Kang (2003) Isolation of proteins that specifically interact with the ATPase domain of mammalian. ER chaperone, BiP. Biotechnol. Bioprocess Eng. 8: 192-198.
22. Dumitru G. L., Y. Groemping, D. Klostermeier, T. Restle, E. Deuerling, and J. Reinstein (2004) DafA cycles between the DnaK chaperone system and translationalmachinery. J. Mol. Biol. 339: 1179-1189.
23. Diamant, S., A. P. Ben-Zvi, B. Bukau, and P. Goloubinoff (2000) Size-dependent disaggregation for stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275: 21107-21113.
24. Gragerov, A., E. Nudler, N. Komissarova, G. A. Gaitanaris, M. E. Gottesman, and V. Nikiforov (1992) Cooperation of GroEL/GroES and DnaK/ DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl. Acad. Sci. USA 89: 10341-10344.
25. Szabo, A., T. Langer, H. Schroder, J. Flanagan, B. Bukau, and F. U. Hartl (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91: 10345-10349.
26. Weissman, J. S., H. S. Rye, W. A. Fenton, J. M. Beechem, and A. L. Horwich (1996) Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84: 481-490.
27. Ying, B. W., H. Taguchi, H. Ueda, and T. Ueda (2004) Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system. Biochem. Biophys. Res. Commun. 320: 1359-1364.
28. Nishihara, K., M. Kanemori, M. Kitagawa, H. Yanagi, and T. Yura (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 64: 1694-1699.
29. Yoon, H. I., Y. J. Choi, O. Miyake, W. Hashimoto, K. Murata, and B. Mikami (2001) Effect of His192 mutation on the activity of alginate lyase A1-III from Sphingomonas species A1. J. Microbiol. Biotechnol. 11: 118-123.
30. Hicks, S. J. and P. Gacesa (1996) Heterologous expression of full-length and truncated forms of the recombinant guluronate-specific alginate lyase of Klebsiella pneumoniae. Enzyme Microb. Technol. 19: 68-73.
31. Gonzalez-Montalban, N., M. M. Carrio, S. Cuatrecasas, A. Aris, and A. Villaverde (2005) Bacterial inclusion bodies are cytotoxic in vivo in absence of functional chaperones DnaK or GroEL. J. Biotechnol. 118: 406-412.
32. Park, S. L., E. J. Shin, S. P. Hong, S. J. Jeon, and S. W. Nam (2004) Production of soluble human granulocyte colony stimulating factor in E. coli by molecular chaperones. J. Microbiol. Biotechnol. 14: 216-219.
33. Chen, Y., J. Song, S. F. Sui, and D. N. Wang (2003) DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli. Protein Expr. Purif. 32: 221-231.
34. Kwak, Y. H., S. J. Kim, K. Y. Lee, and H. B. Kim (2000) Stress responses of the Escherichia coli groE promoter. J. Microbiol. Biotechnol 10: 63-68.