Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Paper
  • Published:

Melanin Production in Escherichia coli from a Cloned Tyrosinase Gene

Bio/Technology volume 8, pages 634–638 (1990)Cite this article

An Erratum to this article was published on 01 August 1990

Abstract

We have cloned and functionally expressed a tyrosinase gene from Streptomyces antibioticus in Escherichia coli under the control of an inducible bacteriophage T7 promoter. Recombinant E. coli cells containing the induced tyrosinase gene produced melanin pigments on agar plates and in liquid culture when supplemented with copper and tyrosine. The expression of an additional open reading frame from the mel gene locus of S. antibioticus was required for high-level melanin production in E. coli. Our results also show that it is possible to screen other classes of precursor compounds for incorporation into melanin pigments with unique colors and other biochemical features. In addition, it may be possible to screen for enhanced melanin production in the absence of added precursors to identify overproducing mutants in the amino acid biosynthetic pathways of E. coli. The ability to screen for a melanin phenotype in recombinant E. coli provides new opportunities for production of novel melanins and for protein engineering of tyrosinases with altered catalytic properties.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Lerch, K. 1981. Copper monooxygenases: tyrosinase and dopamine β-monooxygenase, p. 143–186. In: Metal Ions in Biological Systems, Volume 13. H. Siegel (Ed.). Marcel Dekker, New York, NY.

    Google Scholar 

  2. Robb, D.A. 1984. Tyrosinase, p. 207–240. In: Copper Proteins and Copper Enzymes, Volume 2, R. Lontie (Ed.), CRC Press, Boca Raton, FL.

    Google Scholar 

  3. Ito, S. 1986. Reexamination of the structure of eumelanin. Biochim. Biophys. Acta 883: 155–161.

    Article  CAS  Google Scholar 

  4. Bell, A.A. and Wheeler, M.H. 1986. Biosynthesis and functions of fungal melanins. Ann. Rev. Phytopathol. 24: 411–451.

    Article  CAS  Google Scholar 

  5. Katz, E., Thompson, C.J. and Hopwood, D.A. 1983. Cloning and expression of the tyrosinase gene from Streptomyces antibioticus in Streptomyces lividans. J. General Microbiol. 123: 2703–2714.

    Google Scholar 

  6. Bernan, V., Filpula, D., Herber, W., Bibb, M. and Katz, E. 1985. The nucleotide sequence of the tyrosinase gene from Streptomyces antibioticus and characterization of the gene product. Gene 37: 101–110.

    Article  CAS  Google Scholar 

  7. Lee, Y.-H.W., Chen, B.-F., Wu, S.-Y., Leu, W.-M., Lin, J.-J., Chen, C.C. and Lo, S.J. 1988. A trans-acting gene is required for the phenotypic expression of a tyrosinase gene in Streptomyces. Gene 65: 71–81.

    Article  CAS  Google Scholar 

  8. Huber, M., Hintermann, G. and Lerch, K. 1985. Primary structure of tyrosinase from Streptomyces glaucescens. Biochemistry 24: 6038–6044.

    Article  CAS  Google Scholar 

  9. Huber, M., Huetter, R. and Lerch, K. 1987. The promoter of the Streptomyces glaucescens mel operon. Nucleic Acids Res. 15: 8106.

    Article  CAS  Google Scholar 

  10. Tabor, S. and Richardson, C.C. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA. 82: 1074–1078.

    Article  CAS  Google Scholar 

  11. Nayak, K.K., Pandey, N.K. and Roy, P. 1988. Cloning of tyrosinase gene from Streptomyces lividans in Escherichia coli. Indian J. Biochem. Biophys. 25: 515–517.

    CAS  PubMed  Google Scholar 

  12. Lerch, K. and Ettlinger, L. 1972. Purification and characterization of a tyrosinase from Streptomyces glaucescens. Eur. J. Biochem. 31: 427–437.

    Article  CAS  Google Scholar 

  13. Maniatis, T., Fritsch, E.F. and Sambrook, J. 1982. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory. Cold Spring Harbor, NY.

    Google Scholar 

  14. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.

    Article  CAS  Google Scholar 

  15. Choudary, P.V. 1984. A simple method for rapid kinetic analyses of yeast enzymes in situ. Analyt. Biochem. 138: 425–429.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Biosource Genetics Corporation, 3333 Vaca Valley Parkway, Vacaville, CA, 95688

    Guy della-Cioppa, Stephen J. Garger, Genadie G. Sverlow, Thomas H. Turpen & Laurence K. Grill

Authors
  1. Guy della-Cioppa
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Stephen J. Garger
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Genadie G. Sverlow
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Thomas H. Turpen
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Laurence K. Grill
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

della-Cioppa, G., Garger, S., Sverlow, G. et al. Melanin Production in Escherichia coli from a Cloned Tyrosinase Gene. Nat Biotechnol 8, 634–638 (1990). https://doi.org/10.1038/nbt0790-634

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nbt0790-634

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing