Reference : Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancie...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins.
Cappellini, Enrico [> >]
Jensen, Lars J. [> >]
Szklarczyk, Damian [> >]
Ginolhac, Aurélien [University of Copenhagen > Centre for Geogenetics]
da Fonseca, Rute A. R. [> >]
Stafford, Thomas W. [> >]
Holen, Steven R. [> >]
Collins, Matthew J. [> >]
Orlando, Ludovic [> >]
Willerslev, Eske [> >]
Gilbert, M. Thomas P. [> >]
Olsen, Jesper V. [> >]
Journal of proteome research
Yes (verified by ORBilu)
United States
[en] Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Elephants ; Femur/chemistry ; Fossils ; Mammoths/metabolism ; Molecular Sequence Data ; Proteins/chemistry/classification ; Proteome/analysis/chemistry ; Proteomics/methods ; Sequence Analysis, Protein ; Serum Albumin/chemistry ; Siberia ; Tandem Mass Spectrometry
[en] 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.

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