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Science 13 April 2007:
Vol. 316. no. 5822, pp. 280 - 285
DOI: 10.1126/science.1137614
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Reports

Protein Sequences from Mastodon and Tyrannosaurus Rex Revealed by Mass Spectrometry

John M. Asara,1,2* Mary H. Schweitzer,3 Lisa M. Freimark,1 Matthew Phillips,1 Lewis C. Cantley1,4

Fossilized bones from extinct taxa harbor the potential for obtaining protein or DNA sequences that could reveal evolutionary links to extant species. We used mass spectrometry to obtain protein sequences from bones of a 160,000- to 600,000-year-old extinct mastodon (Mammut americanum) and a 68-million-year-old dinosaur (Tyrannosaurus rex). The presence of T. rex sequences indicates that their peptide bonds were remarkably stable. Mass spectrometry can thus be used to determine unique sequences from ancient organisms from peptide fragmentation patterns, a valuable tool to study the evolution and adaptation of ancient taxa from which genomic sequences are unlikely to be obtained.

1 Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA.
2 Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; North Carolina Museum of Natural Sciences, Raleigh, NC 27601, USA; and Museum of the Rockies, Montana State University, Bozeman, MT 59717, USA.
3 Department of Marine, Earth and Atmospheric Sciences, North Carolina State University, Raleigh, NC 27695, USA.
4 Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.

* To whom correspondence should be addressed. E-mail: jasara{at}bidmc.harvard.edu

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Analyses of Soft Tissue from Tyrannosaurus rex Suggest the Presence of Protein.
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