Peptide sequences from the first Castoroides ohioensis skull and the utility of old museum collections for palaeoproteomics.
Vertebrate fossils have been collected for hundreds of years and are stored in museum collections around the world. These remains provide a readily available resource to search for preserved proteins; however, the vast majority of palaeoproteomic studies have focused on relatively recently collected bones with a well-known handling history. Here, we characterize proteins from the nasal turbinates of the first Castoroides ohioensis skull ever discovered. Collected in 1845, this is the oldest museum-curated specimen characterized using palaeoproteomic tools. Our mass spectrometry analysis detected many collagen I peptides, a peptide from haemoglobin beta, and in vivo and diagenetic post-translational modifications. Additionally, the identified collagen I sequences provide enough resolution to place C. ohioensis within Rodentia. This study illustrates the utility of archived museum specimens for both the recovery of preserved proteins and phylogenetic analyses.
Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA tpcleland@utexas.edu.
Timothy P
0000-0001-9198-2828
TP
Cleland
Department of Biological Sciences, North Carolina State University, Raleigh, NC 27695, USA.
Elena R
ER
Schroeter
New York State Museum, Albany, NY 12230, USA.
Robert S
RS
Feranec
Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Deepak
D
Vashishth
D000818:Animals; D005580:Fossils; D009144:Museums; D010455:Peptides / Q000737:chemistry*; D010802:Phylogeny; D040901:Proteomics; D012377:Rodentia / Q000145:classification*; D012886:Skull
D010455:Peptides
collagen I; museum specimens; nasal turbinates; palaeoproteomics