Overexpression, on-column refolding and isotopic labeling of Hahellin from Hahella chejuensis, a putative member of the βγ-crystallin superfamily

Protein Expression and Purification

Volumn 58, Issue 2, 2008, Pages 269-274

  Srivastava, Atul K ^a   Sharma, Yogendra ^b   Chary, Kandala V R ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

Crystallin; HSQC; Inclusion bodies; Isotopic labeling; M9 minimal media; MALDI TOF; On column refolding; Protein overexpression

Indexed keywords

BACTERIAL PROTEIN; CARBON; CRYSTALLIN; NITROGEN;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CELL INCLUSION; CHEMISTRY; ESCHERICHIA COLI; GAMMAPROTEOBACTERIA; GEL CHROMATOGRAPHY; GENETICS; MASS SPECTROMETRY; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARBON ISOTOPES; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; CRYSTALLINS; ESCHERICHIA COLI; GAMMAPROTEOBACTERIA; INCLUSION BODIES; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; HAHELLA; HAHELLA CHEJUENSIS;

EID: 39549120429     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.12.010     Document Type: Article

References (20)

1. Lubsen N.H., Aarts H.J., and Schoenmakers J.G. The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family. Prog. Biophys. Mol. Biol. 51 (1988) 47-76
2. Jaenicke R., and Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36 (2001) 435-499
3. Bloemendal H., de J.W., Jaenicke R., Lubsen N.H., Slingsby C., and Tardieu A. Aging and vision: structure, stability and function of lens crystallins. Prog. Biophys. Mol. Biol. 86 (2004) 407-485
4. Wistow G. Evolution of a protein superfamily: relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30 (1990) 140-145
5. Jeong H., Yim J.H., Lee C., Choi S.H., Park Y.K., Yoon S.H., Hur C.G., Kang H.Y., Kim D., Lee H.H., Park K.H., Park S.H., Park H.S., Lee H.K., Oh T.K., and Kim J.F. Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent. Nucleic Acids Res. 33 (2005) 7066-7073
6. Lee H.K., Chun J., Moon E.Y., Ko S.H., Lee D.S., Lee H.S., and Bae K.S. Hahella chejuensis gen. nov., sp. nov., an extracellular-polysaccharide-producing marine bacterium. Int. J. Syst. Evol. Microbiol. 51 (2001) 661-666
7. Wistow G., Summers L., and Blundell T. Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens beta gamma-crystallins. Nature 315 (1985) 771-773
8. Wistow G., Turnell B., Summers L., Slingsby C., Moss D., Miller L., Lindley P., and Blundell T. X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution. J. Mol. Biol. 170 (1983) 175-202
9. Graw J. The crystallins: genes, proteins and diseases. Biol. Chem. 378 (1997) 1331-1348
10. Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
11. Grune T., Jung T., Merker K., and Davies K.J. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36 (2004) 2519-2530
12. Valax P., and Georgiou G. Molecular characterization of beta-lactamase inclusion bodies produced in Escherichia coli. 1. Composition. Biotechnol. Prog. 9 (1993) 539-547
13. Singh S.M., and Panda A.K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 99 (2005) 303-310
14. Middelberg A.P. Preparative protein refolding. Trends Biotechnol. 20 (2002) 437-443
15. Jungbauer A., Kaar W., and Schlegl R. Folding and refolding of proteins in chromatographic beds. Curr. Opin. Biotechnol. 15 (2004) 487-494
16. Li M., Su Z.G., and Janson J.C. In vitro protein refolding by chromatographic procedures. Protein Expr. Purif. 33 (2004) 1-10
17. Jobby M.K., and Sharma Y. Purification of a crystallin domain of Yersinia crystallin from inclusion bodies and its comparison to native protein from the soluble fraction. Biomed. Chromatogr. 20 (2006) 956-963
18. Suttnar J., Dyr J.E., Hamsikova E., Novak J., and Vonka V. Procedure for refolding and purification of recombinant proteins from Escherichia coli inclusion bodies using a strong anion exchanger. J. Chromatogr. B Biomed. Appl. 656 (1994) 123-126
19. Sambrook J., et al. Molecular Cloning: A Laboratory Manual A.1. second ed. (1989), Plainview, NY
20. Bai Y., Chung J., Dyson H.J., and Wright P.E. Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions. Protein Sci. 10 (2001) 1056-1066