4.8 Article

Protein sequences bound to mineral surfaces persist into deep time

Journal

ELIFE
Volume 5, Issue -, Pages -

Publisher

ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.17092

Keywords

-

Categories

Funding

  1. Engineering and Physical Sciences Research Council [EP/I001514/1, EP/K000225/1]
  2. Natural Environment Research Council [NERC NE/G004625/1]
  3. Arts and Humanities Research Council [AHRC AH/L006979]
  4. European Research Council [PERG07-GA-2010-268429, SMILEY FP7-NMP-2012-SMALL-6-310637]
  5. Novo Nordisk [NNF14CC0001]
  6. Danish National Research Foundation [DNRF94]
  7. National Science Foundation [BCS-0524087, BCS-1138073, 547414, BCS-9903434, BCS-0309513, BCS-0216683]
  8. Hyde Family Foundations
  9. John Templeton Foundation
  10. Arizona State University
  11. National Geographic Society
  12. Leakey Foundation
  13. Tanzanian Department of Antiquities
  14. Social Sciences and Humanities Research Council of Canada
  15. Leverhulme Trust
  16. Spanish Ministry of Economy and Competitivity [HAR2013-45246-C3-1-P]
  17. Direct For Biological Sciences
  18. Division Of Environmental Biology [1547414] Funding Source: National Science Foundation
  19. Direct For Social, Behav & Economic Scie
  20. Division Of Behavioral and Cognitive Sci [1350023] Funding Source: National Science Foundation
  21. Engineering and Physical Sciences Research Council [EP/K000225/1, EP/I001514/1, EP/L000202/1, EP/K000209/1] Funding Source: researchfish
  22. Natural Environment Research Council [NE/G004625/1] Funding Source: researchfish
  23. Novo Nordisk Foundation Center for Protein Research [PI Jesper Velgaard Olsen] Funding Source: researchfish
  24. EPSRC [EP/K000225/1, EP/L000202/1, EP/I001514/1, EP/K000209/1] Funding Source: UKRI
  25. 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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