As part of the ongoing celebration of the last 25 years of Nature Genetics, the editors are each choosing a few papers from our archives that we want to highlight. My first pick a paper from Kevin Campbell, Alan Cooper and colleagues on their structure-function analysis of woolly mammoth hemoglobin, published in May 2010.
I’ve picked this one to highlight because, well, who doesn’t love woolly mammoths?
The authors compared the gene sequences of the adult-expressed α- and β-like globin genes from extant elephant species (African and Asian elephants) and from a 43,000 year-old Siberian mammoth specimen reported first in Science. They found that the mammoth β-like genes (designated HBB/HBD by the authors) had 3 amino acid-altering substitutions compared to the extant species.
To test the effects of these protein-coding differences, the authors then “resurrected” the mammoth hemoglobin protein by expressing the mammoth sequence in E. coli and testing its O2 affinity at different ambient temperatures. They found that the O2 affinity of the recreated mammoth hemoglobin is less affected by temperature than that of modern-day elephants. The detailed structure-function analysis reported by Campbell et al. offered us a rare glimpse into the evolutionary process that shaped an extinct organism.