A simple, rapid method for the production of soluble recombinant proteins from the duplicated growth hormone genes of the tetraploid common carp

• Autorzy: Murakaeva A. , Kohlmann K.
• Języki publikacji: EN

Abstrakty

EN

The simple protein production method developed in the present study enables the production of large quantities of active recombinant common-carp growth hormone proteins in a few brief steps. With this method, the recombinant protein is obtained in a soluble form without the need for refolding. This method can be utilised for determining if the two common-carp growth hormones have similar functions in vitro and in vivo and what role each plays in growth regulation. If differences in activity exist, this method can also be used to produce intermediate forms of the two common carp growth hormones rapidly in order to determine which of the six amino acids that differ between the two proteins are responsible for the altered activity. Common carp has the same tetraploid ancestor as goldfish, and the products of the growth hormone paralogues in goldfish also differ. It would be interesting to understand how the same duplicated orthologues have evolved, and the methods elaborated in this study could be used for such comparative investigations.

Słowa kluczowe

EN

common carp; gene duplication; genome duplication; growth hormone

PL

karp; powielanie genu; powielanie genomu; hormon wzrostu

• Wydawca: University of Warmia and Mazury in Olsztyn, Poland
• Czasopismo: Environmental Biotechnology
• Rocznik: 2011
• Tom: Vol. 7, No. 2
• Strony: 53--64
• Opis fizyczny: Bibliogr. 43 poz., rys., tab., wykr.

Twórcy

autor

Murakaeva A.

autor

Kohlmann K.

• Leibniz-Institute of Freshwater Ecology and Inland Fisheries, Müggelseedamm 310, 12587 Berlin, Germany,

Bibliografia

• Aslund, F., P.H. Bessette, G. Georgiou, J. Beckwith. 1999. Efficient Production of Disulfide Bonded Proteins in the Cytoplasm in “Oxidizing” Mutants of E. coli. inNovations 10: 11-12.
• Bailey, G.S., R.T.M. Poulter, P.A. Stockwell. 1978. Gene duplication in tetraploid fish:Model for gene silencing at unlinked duplicated loci. Proceedings of the National Academy of Sciences 75: 5575-5579.
• Bessette, P.H., F. Aslund, J. Beckwith, G. Georgiou. 1999. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proceedings of the National Academy of Sciences 96: 13703-13708.
• Bowden, G.A., G. Georgiou. 1990. Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli. Journal of Biological Chemistry 265: 16760-16766.
• Brinkmann, U., R.E. Mattes, P. Buckel. 1989. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85: 109-114.
• Chalmers, J.J., E. Kim, J.N. Telford, E.Y. Wong, W.C. Tacon, M.L. Shuler, D.B. Wilson. 1990. Effects of temperature on Escherichia coli overproducing β-lactamase or human epidermal growth factor. Applied and Environmental Microbiology 56: 104-111.
• Charrier, J., J. Martal. 1988. Growth hormones. 1. Polymorphism. (Minireview). Reproduction Nutrition Development 28: 857-887.
• Collins-Racie, L.A. J.M. McColgan, K.L. Grant, E.A. DiBlasio-Smith, J.M. McCoy, E.R. LaVallie. 1995. Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA. Biotechnology 13: 982-987.
• FAO Fishery Statistics, 2008. available at ftp://ftp.fao.org/FI/CDrom/CD_yearbook_2008/navigation/index_content_aquaculture_e.htm
• Fine, M., E. Sakal, D. Vashdi, V. Daniel, A. Levanon, O. Lipshitz, A. Gertler. 1993. Recombinant carp (Cyprinus carpio) growth hormone: expression, purification, and determination of biological activity in vitro and in vivo. General and Comparative Endocrinology 89: 51-61.
• Futami, K., T. Komiya, H. Zhang, N. Okamoto. 2001. Differential expression of max and two types of c-myc genes in a tetraploid fish, the common carp (Cyprinus carpio). Gene 269: 113-119.
• Futami, K., H. Zhang, N. Okamoto. 2005. Functional divergence of duplicated c-myc genes in a tetraploid fish, the common carp (Cyprinus carpio). Gene 363: 61-66.
• Grodberg, J., J.J. Dunn. 1988. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. Journal of Bacteriology 170: 1245-1253.
• Hochuli, E., H. Döbeli, A. Schacher. 1987. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. Journal of Chromatography 411: 177-184.
• Hochuli, E., W. Bannwarth, R. Döbeli, R. Gentz, D. Stüber. 1988. Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. BioTechnology 6: 1321-1325.
• Hughes, M.K., A.L. Hughes. 1993. Evolution of duplicate genes in a tetraploid animal, Xenopus laevis. Molecular Biology Evolution 10: 1360-1369.
• Hughes, A.L., T. Ota, M. Nei. 1990. Positive Darwinian selection promotes charge profile diversity in the antigen-binding cleft of class I major-histocompatibility-complex molecules. Molecular Biology Evolution 7: 515-524.
• Kane, J.F. 1995. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Current Opinion in Biotechnology 6: 494-500.
• Kopetzki, E., G. Schumacher, P. Buckel. 1989. Control of formation of active soluble or inactive insoluble baker's yeast alphaglucosidase PI in Escherichia coli by induction and growth conditions. Molecular Genetics and Genomics 216: 149-155.
• Kurland, C., J. Gallant. 1996. Errors of heterologous protein expression. Current Opinion in Biotechnology 7: 489-493.
• LaVallie, E.R., E.A. DiBlasio, S. Kovacic, K.L. Grant, P.F. Schendel, J.M. McCoy. 1993. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. BioTechnology 11: 187-193.
• Larhammar, D., L.-G. Lundin, F. Hallböök. 2002. The human Hoxbearing chromosome regions did arise by block or chromosome (or even genome) duplications. Genome Research 12: 1910-1920.
• McLysaght, A., K. Hokamp, K.H. Wolfe. 2002. Extensive genomic duplication during early chordate evolution. Nature Genetics 31: 200-204.
• Murakaeva, A. 2008. Structure, evolution and expression of the duplicated growth hormone genes of common carp (Cyprinus carpio). Dissertation Thesis, Humboldt-University of Berlin, Germany.
• Nadeau, J.H., D. Sankoff. 1997. Comparable rates of gene loss and functional divergence after genome duplication early in vertebrate evolution. Genetics 147: 1259-1266.
• Nygren, P.-A., S. Stahl, M. Uhlen. 1994. Engineering proteins to facilitate bioprocessing. Trends in Biotechnology 12: 184-188.
• Ohno, S. 1970. Evolution by gene duplication. 160 p. George Allen & Unwin, London.
• Prinz, W.A., F. Aslund, A. Holmgren, J. Beckwith. 1997. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. Journal of Biological Chemistry 272: 15661-15667.
• Sambrook, J., E.F. Fritsch, T. Maniatis. 1989. Molecular cloning. A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
• Schein, C.H. 1989. Production of soluble recombinant proteins in bacteria. BioTechnology 7: 1141-1148.
• Schmid, A.,W. Kloas,M. Reinecke. 1999. Establishment of a primary liver cell culture from a teleost, Oreochromis mossambicus, the tilapia: A valid tool for physiological studies. Proceedings of the 16th ESACT Meeting. Lugano, Switzerland, April 25th to 29th 1999: 1-3.
• Schmid, A., M. Reinecke, W. Kloas. 2000. Primary cultured hepatocytes of the bony fish, Oreochromis mossambicus, the tilapia: A valid tool for physiological studies on insulin-like growth factor-I (IGF-I) expression in liver. Journal of Endocrinology 166: 265-273.
• SCR3 program: available on the website of the «Hughes Lab Bioinformatics Resource» at http://www.biol.sc.edu/~austin/
• Seidel, H.M., D.L. Pompliano, J.R. Knowles. 1992. Phosphonate biosynthesis: molecular cloning of the gene for phosphoenolpyruvate mutase from Tetrahymena pyriformis and overexpression of the gene product in Escherichia coli. Biochemistry 31: 2598-2608.
• Shatzman, A.R. 1990. Gene expression using gram-negative bacteria. Current Opinion in Biotechnology 1: 5-11.
• Shih, Y.P., W.M. Kung, J.C. Chen, J.H. Yeh, A.H.J. Wang, T.F. Wang. 2002. High throughput screening of soluble recombinant proteins. Protein Science 1714-1719.
• Smith, M.C., C. Pidgeon. 1986. Process for purifying proteins and compounds useful in such process. U.S. Patent No. 4,569,794.
• Smith, M.C., T.C. Furman, C. Pidgeon. 1987. Immobilized iminodiacetic acid metal peptide complexes. Identification of chelating peptide purification handles for recombinant proteins. Inorganic Chemistry 26: 1965-1969.
• Stewart, E.J., F. Aslund, J. Beckwith. 1998. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal or the thioredoxins. The EMBO Journal 17: 5543-5550.
• Strandberg, L., S.O. Enfors. 1991. Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Applied and Environmental Microbiology 57: 1669-1674.
• Studier, F.W., B.A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. Journal of Molecular Biology 189: 113-130.
• Tajima, F. 1993. Simple methods for testing the molecular evolutionary clock hypothesis. Genetics 135: 599-607.
• Zheng, L.,U. Baumann, J.L.Reymond. 2003. Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm. Journal of Biochemistry 133: 577-581.