Protein sequences bound to mineral surfaces persist into deep time
peer-reviewed · eLife · 2016
| Date | 2016-09-27 |
| Type | peer-reviewed |
| Venue | eLife |
| Publisher | eLife Sciences Publications, Ltd |
| Contribution | downstream-application |
| DOI | 10.7554/eLife.17092 |
| Citations (OpenAlex) | 278 |
| Venue 2-year citedness | 1.79 |
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).
Methods and tools
- Ancient ostrich eggshell proteome: Sequencing of ancient peptides bound to ostrich eggshell mineral surfaces, demonstrating protein survival into deep time (~3.8 million years) via de novo MS/MS workflows.
Data used
- Mineral-bound ostrich eggshell peptides survive for up to 3.8 Ma in equatorial Africa (as deposited) · PXD003786
Cites (1)
Cited by (9)
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