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.

  • NEWS AND VIEWS

Extinct proteins resurrected to reconstruct the evolution of vertebrate haemoglobin

The multi-subunit protein haemoglobin relies on complex interactions between its components to function properly. Analysis of ancient precursors suggests that its evolution from a simple monomer involved only a few steps.
  1. Michael Berenbrink

    1. Michael Berenbrink is in the Department of Evolution, Ecology and Behaviour, University of Liverpool, Liverpool L69 7ZB, UK.

    View author publications

    You can also search for this author in PubMed  Google Scholar

The oxygen-transporting protein haemoglobin has under gone repeated adaptations as animals evolved to conquer new environments — from the depths of the oceans1 to high mountain ranges2. These adaptations relied on changes in the long-range interactions between oxygen-binding sites buried in the protein’s subunits, and between these regions and binding sites for a multitude of small effector molecules on the protein’s surface3. How did this complex molecular machine, which can respond so exquisitely to available levels of both oxygen and several other effector molecules, come into being? Writing in Nature, Pillai et al.4 reconstruct the stepwise evolution of haemoglobin from precursors that existed more than 400 million years ago.

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Learn more

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

Nature 581, 388-389 (2020)

doi: https://doi.org/10.1038/d41586-020-01287-8

References

  1. Berenbrink, M., Koldkjær, P., Kepp, O. & Cossins, A. R. Science 307, 1752–1757 (2005).

    Article  PubMed  Google Scholar 

  2. Natarajan, C. et al. Science 354, 336–339 (2016).

    Article  PubMed  Google Scholar 

  3. Perutz, M. F. Mol. Biol. Evol. 1, 1–28 (1983).

    PubMed  Google Scholar 

  4. Pillai, A. S. et al. Nature 581, 480–485 (2020).

    Article  Google Scholar 

  5. Antonini, E. & Brunori, M. Hemoglobin and Myoglobin in Their Reactions with Ligands 21 (North-Holland, 1971).

    Google Scholar 

  6. Benner, S. A. in Ancestral Sequence Reconstruction (ed. Liberles, D. A.) Ch. 1, 3–19 (Oxford Univ. Press, 2007).

    Google Scholar 

  7. Krogh, A. & Leitch, I. J. Physiol. (Lond.) 52, 288–300 (1919).

    Article  PubMed  Google Scholar 

  8. Storz, J. F. Hemoglobin: Insights into Protein Structure, Function, and Evolution (Oxford Univ. Press, 2019).

    Google Scholar 

  9. Imai, K. Allosteric Effects in Haemoglobin (Cambridge Univ. Press, 1982).

    Google Scholar 

  10. Schachat, S. R. et al. Proc. R. Soc. B 285, 20172631 (2018).

    Article  PubMed  Google Scholar 

  11. Rund, D. & Rachmilewitz, E. N. Engl. J. Med. 353, 1135–1146 (2005).

    Article  PubMed  Google Scholar 

  12. Mirceta, S. et al. Science 340, 1234192 (2013).

    Article  PubMed  Google Scholar 

  13. Zuckerkandl, E. in Ancestral Sequence Reconstruction (ed. Liberles, D. A.) x–xi (Oxford Univ. Press, 2007).

    Google Scholar 

Download references

Subjects

Latest on:

Nature Careers

Jobs

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

Search

Advanced search

Quick links