Journal
ELIFE
Volume 5, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.17092
Keywords
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Categories
Funding
- Engineering and Physical Sciences Research Council [EP/I001514/1, EP/K000225/1]
- Natural Environment Research Council [NERC NE/G004625/1]
- Arts and Humanities Research Council [AHRC AH/L006979]
- European Research Council [PERG07-GA-2010-268429, SMILEY FP7-NMP-2012-SMALL-6-310637]
- Novo Nordisk [NNF14CC0001]
- Danish National Research Foundation [DNRF94]
- National Science Foundation [BCS-0524087, BCS-1138073, 547414, BCS-9903434, BCS-0309513, BCS-0216683]
- Hyde Family Foundations
- John Templeton Foundation
- Arizona State University
- National Geographic Society
- Leakey Foundation
- Tanzanian Department of Antiquities
- Social Sciences and Humanities Research Council of Canada
- Leverhulme Trust
- Spanish Ministry of Economy and Competitivity [HAR2013-45246-C3-1-P]
- Direct For Biological Sciences
- Division Of Environmental Biology [1547414] Funding Source: National Science Foundation
- Direct For Social, Behav & Economic Scie
- Division Of Behavioral and Cognitive Sci [1350023] Funding Source: National Science Foundation
- Engineering and Physical Sciences Research Council [EP/K000225/1, EP/I001514/1, EP/L000202/1, EP/K000209/1] Funding Source: researchfish
- Natural Environment Research Council [NE/G004625/1] Funding Source: researchfish
- Novo Nordisk Foundation Center for Protein Research [PI Jesper Velgaard Olsen] Funding Source: researchfish
- EPSRC [EP/K000225/1, EP/L000202/1, EP/I001514/1, EP/K000209/1] Funding Source: UKRI
- NERC [NE/G004625/1] Funding Source: UKRI
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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 thepalaeontological 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 similar to 16 Ma at a constant 10 degrees C).
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