Protein sequences bound to mineral surfaces persist into deep time.
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Authors
Hall, Shaun
Roncal-Herrero, Teresa
Freeman, Colin L
Woolley, Jos
Crisp, Molly K
Wilson, Julie
Fotakis, Anna
Fischer, Roman
Kessler, Benedikt M
Rakownikow Jersie-Christensen, Rosa
Olsen, Jesper V
Haile, James
Thomas, Jessica
Marean, Curtis W
Parkington, John
Presslee, Samantha
Lee-Thorp, Julia
Ditchfield, Peter
Hamilton, Jacqueline F
Ward, Martyn W
Wang, Chunting Michelle
Shaw, Marvin D
Harrison, Terry
Domínguez-Rodrigo, Manuel
MacPhee, Ross DE
Kwekason, Amandus
Kolska Horwitz, Liora
Chazan, Michael
Kröger, Roland
Thomas-Oates, Jane
Harding, John H
Cappellini, Enrico
Penkman, Kirsty
Collins, Matthew J
Publication Date
2016-09-27Journal Title
Elife
ISSN
2050-084X
Publisher
eLife Sciences Publications, Ltd
Volume
5
Language
eng
Type
Article
Physical Medium
Electronic
Metadata
Show full item recordCitation
Demarchi, B., Hall, S., Roncal-Herrero, T., Freeman, C. L., Woolley, J., Crisp, M. K., Wilson, J., et al. (2016). Protein sequences bound to mineral surfaces persist into deep time.. Elife, 5 https://doi.org/10.7554/eLife.17092
Abstract
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).
Keywords
Struthio camelus, biochemistry, biomineralization, eggshell, evolutionary biology, genomics, molecular dynamics, paleontology, paleoproteomics
Sponsorship
Directorate for Biological Sciences (1547414)
Arts and Humanities Research Council (AH/L006979/1)
Natural Environment Research Council (NE/G004625/1)
Identifiers
External DOI: https://doi.org/10.7554/eLife.17092
This record's URL: https://www.repository.cam.ac.uk/handle/1810/285855
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