Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins

Publikation: Bidrag til tidsskriftTidsskriftartikel

Enrico Cappellini, Lars Juhl Jensen, Damian Milosz Szklarczyk, Aurélien Ginolhac, Rute Andreia Rodrigues da Fonseca, Thomas Stafford jr., Steven R. Holen, Matthew J. Collins, Ludovic Antoine Alexandre Orlando, Eske Willerslev, Tom Gilbert, Jesper Velgaard Olsen

We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun sequence ancient protein remains extracted from a 43 000 year old woolly mammoth (Mammuthus primigenius) bone preserved in the Siberian permafrost. For the first time, 126 unique protein accessions, mostly low-abundance extracellular matrix and plasma proteins, were confidently identified by solid molecular evidence. Among the best characterized was the carrier protein serum albumin, presenting two single amino acid substitutions compared to extant African (Loxodonta africana) and Indian (Elephas maximus) elephants. Strong evidence was observed of amino acid modifications due to post-mortem hydrolytic and oxidative damage. A consistent subset of this permafrost bone proteome was also identified in more recent Columbian mammoth (Mammuthus columbi) samples from temperate latitudes, extending the potential of the approach described beyond subpolar environments. Mass spectrometry-based ancient protein sequencing offers new perspectives for future molecular phylogenetic inference and physiological studies on samples not amenable to ancient DNA investigation. This approach therefore represents a further step into the ongoing integration of different high-throughput technologies for identification of ancient biomolecules, unleashing the field of paleoproteomics.
OriginalsprogEngelsk
TidsskriftJournal of Proteome Research
Vol/bind11
Udgave nummer2
Sider (fra-til)917-926
Antal sider10
ISSN1535-3893
DOI
StatusUdgivet - 2012

ID: 48848581