TY - JOUR
T1 - Protein sequences bound to mineral surfaces persist into deep time
AU - Demarchi, Beatrice
AU - Hall, Shaun
AU - Roncal-Herrero, Teresa
AU - Freeman, Colin L.
AU - Woolley, Jos
AU - Crisp, Molly K.
AU - Wilson, Julie
AU - Fotakis, Anna Katerina
AU - Fischer, Roman
AU - Kessler, Benedikt M.
AU - Jersie-Christensen, Rosa Rakownikow
AU - Olsen, Jesper Velgaard
AU - Haile, James
AU - Thomas, Jessica
AU - Marean, Curtis W.
AU - Parkington, John
AU - Presslee, Samantha
AU - Lee-Thorp, Julia
AU - Ditchfield, Peter
AU - Hamilton, Jacqueline F.
AU - Ward, Martyn W.
AU - Wang, Chunting Michelle
AU - Shaw, Marvin D.
AU - Harrison, Terry
AU - Domínguez-Rodrigo, Manuel
AU - MacPhee, Ross D. E.
AU - Kwekason, Amandus
AU - Ecker, Michaela
AU - Kolska Horwitz, Liora
AU - Chazan, Michael
AU - Kröger, Roland
AU - Thomas-Oates, Jane
AU - Harding, John H.
AU - Cappellini, Enrico
AU - Penkman, Kirsty
AU - Collins, Matthew James
PY - 2016
Y1 - 2016
N2 - Proteins persist longer in the fossil record than DNA, but the longevity, survival mechanisms and substrates remain contested. Here, we demonstrate the role of mineral binding in preserving the protein sequence in ostrich (Struthionidae) eggshell, including from the palaeontological sites of Laetoli (3.8 Ma) and Olduvai Gorge (1.3 Ma) in Tanzania. By tracking protein diagenesis back in time we find consistent patterns of preservation, demonstrating authenticity of the surviving sequences. Molecular dynamics simulations of struthiocalcin-1 and -2, the dominant proteins within the eggshell, reveal that distinct domains bind to the mineral surface. It is the domain with the strongest calculated binding energy to the calcite surface that is selectively preserved. Thermal age calculations demonstrate that the Laetoli and Olduvai peptides are 50 times older than any previously authenticated sequence (equivalent to ~16 Ma at a constant 10°C).
AB - Proteins persist longer in the fossil record than DNA, but the longevity, survival mechanisms and substrates remain contested. Here, we demonstrate the role of mineral binding in preserving the protein sequence in ostrich (Struthionidae) eggshell, including from the palaeontological sites of Laetoli (3.8 Ma) and Olduvai Gorge (1.3 Ma) in Tanzania. By tracking protein diagenesis back in time we find consistent patterns of preservation, demonstrating authenticity of the surviving sequences. Molecular dynamics simulations of struthiocalcin-1 and -2, the dominant proteins within the eggshell, reveal that distinct domains bind to the mineral surface. It is the domain with the strongest calculated binding energy to the calcite surface that is selectively preserved. Thermal age calculations demonstrate that the Laetoli and Olduvai peptides are 50 times older than any previously authenticated sequence (equivalent to ~16 Ma at a constant 10°C).
U2 - 10.7554/eLife.17092
DO - 10.7554/eLife.17092
M3 - Journal article
C2 - 27668515
VL - 5
JO - eLife
JF - eLife
SN - 2050-084X
M1 - e17092
ER -