Peptide sequences from the first Castoroides ohioensis skull and the utility of old museum collections for palaeoproteomics

Author:

Cleland Timothy P.1ORCID,Schroeter Elena R.2,Feranec Robert S.3,Vashishth Deepak1

Affiliation:

1. Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA

2. Department of Biological Sciences, North Carolina State University, Raleigh, NC 27695, USA

3. New York State Museum, Albany, NY 12230, USA

Abstract

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.

Funder

National Science Foundation

Publisher

The Royal Society

Subject

General Agricultural and Biological Sciences,General Environmental Science,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine

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