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
AU - Woolley, Jos
AU - Crisp, Molly Katherine
AU - Wilson, Julie Carol
AU - Fotakis, Anna
AU - Fischer, Roman
AU - Kessler, Benedikt
AU - Rakownikow Jersie-Christensen, Rosa
AU - Olsen, Jesper
AU - Haile, James
AU - Thomas, Jessica
AU - Marean, Curtis
AU - Parkington, John
AU - Presslee, Samantha Louise
AU - Lee-Thorp, Julia
AU - Ditchfield, Peter
AU - Hamilton, Jacqueline Fiona
AU - Ward, Martyn William
AU - Wang, Chunting Michelle
AU - Shaw, Marvin David
AU - Harrison, Terry
AU - Dominguez-Rodrigo, Manuel
AU - MacPhee, Ross
AU - Kwekason, Amandus
AU - Ecker, Michaela
AU - Kolska Horwitz, Liora
AU - Chazan, Michael
AU - Kröger, Roland
AU - Thomas-Oates, Jane Elizabeth
AU - Harding, John
AU - Cappellini, Enrico
AU - Penkman, Kirsty Elizabeth Helena
AU - Collins, Matthew James
PY - 2016/9/27
Y1 - 2016/9/27
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).
UR - http://www.scopus.com/inward/record.url?scp=84988893010&partnerID=8YFLogxK
U2 - 10.7554/eLife.17092
DO - 10.7554/eLife.17092
M3 - Article
C2 - 27668515
SN - 2050-084X
VL - 5
SP - 1
EP - 50
JO - eLife
JF - eLife
IS - September
M1 - e17092
ER -