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.

  • Feature
  • Published:

More bright ideas

Nature Biotechnology volume 24, pages 304–305 (2006)Cite this article

It's easy to forget that the complex applications and permutations began with a small, bioluminescent jellyfish that lives off the coast of Washington State. Over a decade ago, Douglas Prasher and colleagues showed that green fluorescent protein (GFP) from Aequorea victoria could be used to track gene expression without any need for exogenous substrates or cofactors1. However, the technique had practical limitations.

For one thing, natural GFP emits too little light to be efficient for tracking proteins in eukaryotic cells. By shuffling GFP DNA in Escherichia coli and selecting for the brightest colonies, Willem Stemmer and colleagues boosted the protein's signal about 40-fold and created a more soluble protein to boot2. That same year, George Phillips and his colleagues solved a high-resolution structure of GFP3. The structure showed the fluorophore near the center of a barrel-like β-can fold and identified several adjacent amino acids that affect spectral properties, opening the door to rational engineering and mutagenesis.

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

References

  1. Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W. & Prasher, D.C. Green fluorescent protein as a marker for gene expression. Science 263, 802–805 (1994).

    Article  CAS  Google Scholar 

  2. Crameri, A., Whitehorn, E.A., Tate, E. & Stemmer, W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315–319 (1996).

    Article  CAS  Google Scholar 

  3. Yang, F., Moss, L.G. & Phillips, G.N. Jr. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14, 1246–1251 (1996).

    Article  CAS  Google Scholar 

  4. Matz, M.V. et al. Fluorescent proteins from nonbioluminescent Anthozoa species. Nat. Biotechnol. 17, 969–973 (1999).

    Article  CAS  Google Scholar 

  5. Nagai, T. et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87–90 (1999).

    Article  Google Scholar 

  6. Bevis, B.J. & Glick, B.S. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat. Biotechnol. 20, 83–87 (2002).

    Article  CAS  Google Scholar 

  7. Chudakov, D.M. et al. Photoswitchable cyan fluorescent protein for protein tracking. Nat. Biotechnol. 22, 1435–1439 (2004).

    Article  CAS  Google Scholar 

  8. Bulina, M.E. et al. A genetically encoded photosensitizer. Nat. Biotechnol. 24, 95–99 (2006).

    Article  CAS  Google Scholar 

Download references

Rights and permissions

Reprints and permissions

About this article

Cite this article

More bright ideas. Nat Biotechnol 24, 304–305 (2006). https://doi.org/10.1038/nbt0306-304

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nbt0306-304

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