eLife (Sep 2016)
Protein sequences bound to mineral surfaces persist into deep time
- Beatrice Demarchi,
- Shaun Hall,
- Teresa Roncal-Herrero,
- Colin L Freeman,
- Jos Woolley,
- Molly K Crisp,
- Julie Wilson,
- Anna Fotakis,
- Roman Fischer,
- Benedikt M Kessler,
- Rosa Rakownikow Jersie-Christensen,
- Jesper V Olsen,
- James Haile,
- Jessica Thomas,
- Curtis W Marean,
- John Parkington,
- Samantha Presslee,
- Julia Lee-Thorp,
- Peter Ditchfield,
- Jacqueline F Hamilton,
- Martyn W Ward,
- Chunting Michelle Wang,
- Marvin D Shaw,
- Terry Harrison,
- Manuel Domínguez-Rodrigo,
- Ross DE MacPhee,
- Amandus Kwekason,
- Michaela Ecker,
- Liora Kolska Horwitz,
- Michael Chazan,
- Roland Kröger,
- Jane Thomas-Oates,
- John H Harding,
- Enrico Cappellini,
- Kirsty Penkman,
- Matthew J Collins
Affiliations
- Beatrice Demarchi
- ORCiD
- BioArCh, Department of Archaeology, University of York, York, United Kingdom
- Shaun Hall
- Department of Material Science and Engineering, University of Sheffield, Sheffield, United Kingdom
- Teresa Roncal-Herrero
- Department of Physics, University of York, York, United Kingdom
- Colin L Freeman
- Department of Material Science and Engineering, University of Sheffield, Sheffield, United Kingdom
- Jos Woolley
- BioArCh, Department of Archaeology, University of York, York, United Kingdom
- Molly K Crisp
- Department of Chemistry, University of York, York, United Kingdom
- Julie Wilson
- Department of Chemistry, University of York, York, United Kingdom; Department of Mathematics, University of York, York, United Kingdom
- Anna Fotakis
- Centre for GeoGenetics, Natural History Museum of Denmark, University of Copenhagen, Copenhagen, Denmark
- Roman Fischer
- Advanced Proteomics Facility, Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom
- Benedikt M Kessler
- Advanced Proteomics Facility, Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Oxford, United Kingdom
- Rosa Rakownikow Jersie-Christensen
- Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark
- Jesper V Olsen
- Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark
- James Haile
- Research Laboratory for Archaeology and the History of Art, University of Oxford, Oxford, United Kingdom
- Jessica Thomas
- Centre for GeoGenetics, Natural History Museum of Denmark, University of Copenhagen, Copenhagen, Denmark; Molecular Ecology and Fisheries Genetics Laboratory, School of Biological Sciences, Bangor University, Bangor, United Kingdom
- Curtis W Marean
- Institute of Human Origins, SHESC, Arizona State University, Tempe, United States; Centre for Coastal Palaeoscience, Nelson Mandela Metropolitan University, Port Elizabeth, South Africa
- John Parkington
- Department of Archaeology, University of Cape Town, Cape Town, South Africa
- Samantha Presslee
- BioArCh, Department of Archaeology, University of York, York, United Kingdom
- Julia Lee-Thorp
- Research Laboratory for Archaeology and the History of Art, University of Oxford, Oxford, United Kingdom
- Peter Ditchfield
- Research Laboratory for Archaeology and the History of Art, University of Oxford, Oxford, United Kingdom
- Jacqueline F Hamilton
- Wolfson Atmospheric Chemistry Laboratories, Department of Chemistry, University of York, York, United Kingdom
- Martyn W Ward
- Wolfson Atmospheric Chemistry Laboratories, Department of Chemistry, University of York, York, United Kingdom
- Chunting Michelle Wang
- Wolfson Atmospheric Chemistry Laboratories, Department of Chemistry, University of York, York, United Kingdom
- Marvin D Shaw
- Wolfson Atmospheric Chemistry Laboratories, Department of Chemistry, University of York, York, United Kingdom
- Terry Harrison
- Center for the Study of Human Origins, Department of Anthropology, New York University, New York, United States
- Manuel Domínguez-Rodrigo
- Department of Prehistory, Complutense University of Madrid, Madrid, Spain
- Ross DE MacPhee
- Department of Mammalogy, American Museum of Natural History, New York, United States
- Amandus Kwekason
- National Museum of Tanzania, Dar es Salaam, Tanzania
- Michaela Ecker
- ORCiD
- Research Laboratory for Archaeology and the History of Art, University of Oxford, Oxford, United Kingdom
- Liora Kolska Horwitz
- National Natural History Collections, Faculty of Life Sciences, The Hebrew University, Jerusalem, Israel
- Michael Chazan
- Department of Anthropology, University of Toronto, Toronto, Canada; Evolutionary Studies Institute, University of the Witwatersrand, Braamfontein, South Africa
- Roland Kröger
- Department of Physics, University of York, York, United Kingdom
- Jane Thomas-Oates
- Department of Chemistry, University of York, York, United Kingdom; Centre of Excellence in Mass Spectrometry, University of York, New York, United States
- John H Harding
- Department of Material Science and Engineering, University of Sheffield, Sheffield, United Kingdom
- Enrico Cappellini
- Centre for GeoGenetics, Natural History Museum of Denmark, University of Copenhagen, Copenhagen, Denmark
- Kirsty Penkman
- Department of Chemistry, University of York, York, United Kingdom
- Matthew J Collins
- BioArCh, Department of Archaeology, University of York, York, United Kingdom
- DOI
- https://doi.org/10.7554/eLife.17092
- Journal volume & issue
-
Vol. 5
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
