Sequence preservation of osteocalcin protein and mitochondrial DNA in bison bones older than 55 ka

TY - JOUR

T1 - Sequence preservation of osteocalcin protein and mitochondrial DNA in bison bones older than 55 ka

AU - Nielsen-Marsh, Christina M.

AU - Ostrom, Peggy H.

AU - Gandhi, Hasand

AU - Shapiro, Beth

AU - Cooper, Alan

AU - Hauschka, Peter V.

AU - Collins, Matthew J.

PY - 2002/12/1

Y1 - 2002/12/1

N2 - We report the first complete sequences of the protein osteocalcin from small amounts (20 mg) of two bison bone (Bison priscus) dated to older than 55.6 ka and older than 58.9 ka. Osteocalcin was purified using new gravity columns (never exposed to protein) followed by microbore reversed-phase high-performance liquid chromatography. Sequencing of osteocalcin employed two methods of matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS): peptide mass mapping (PMM) and post-source decay (PSD). The PMM shows that ancient and modern bison osteocalcin have the same mass to charge (m/z) distribution, indicating an identical protein sequence and absence of diagenetic products. This was confirmed by PSD of the m/z 2066 tryptic peptide (residues 1-19); the mass spectra from ancient and modern peptides were identical. The 129 mass unit difference in the molecular ion between cow (Bos taurus) and bison is caused by a single amino-acid substitution between the taxa (Trp in cow is replaced by Gly in bison at residue 5). Bison mitochondrial control region DNA sequences were obtained from the older than 55.6 ka fossil. These results suggest that DNA and protein sequences can be used to directly investigate molecular phylogenies over a considerable time period, the absolute limit of which is yet to be determined.

AB - We report the first complete sequences of the protein osteocalcin from small amounts (20 mg) of two bison bone (Bison priscus) dated to older than 55.6 ka and older than 58.9 ka. Osteocalcin was purified using new gravity columns (never exposed to protein) followed by microbore reversed-phase high-performance liquid chromatography. Sequencing of osteocalcin employed two methods of matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS): peptide mass mapping (PMM) and post-source decay (PSD). The PMM shows that ancient and modern bison osteocalcin have the same mass to charge (m/z) distribution, indicating an identical protein sequence and absence of diagenetic products. This was confirmed by PSD of the m/z 2066 tryptic peptide (residues 1-19); the mass spectra from ancient and modern peptides were identical. The 129 mass unit difference in the molecular ion between cow (Bos taurus) and bison is caused by a single amino-acid substitution between the taxa (Trp in cow is replaced by Gly in bison at residue 5). Bison mitochondrial control region DNA sequences were obtained from the older than 55.6 ka fossil. These results suggest that DNA and protein sequences can be used to directly investigate molecular phylogenies over a considerable time period, the absolute limit of which is yet to be determined.

KW - Bison

KW - DNA

KW - Fossils

KW - Mass spectrometry

KW - Preservation

KW - Proteins

UR - http://www.scopus.com/inward/record.url?scp=0347925081&partnerID=8YFLogxK

U2 - 10.1130/0091-7613(2002)030<1099:SPOOPA>2.0.CO;2

DO - 10.1130/0091-7613(2002)030<1099:SPOOPA>2.0.CO;2

M3 - Journal article

AN - SCOPUS:0347925081

SN - 0091-7613

VL - 30

SP - 1099

EP - 1102

JO - Geology

JF - Geology

IS - 12

ER -