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Protein sequences bound to mineral surfaces persist into deep time
- Source :
- Elife (2050-084X) (Elife Sciences Publications Ltd), 2016-09 , Vol. 5 , N. e17092 , P. 1-50
- Publication Year :
- 2016
-
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 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).
Details
- Database :
- OAIster
- Journal :
- Elife (2050-084X) (Elife Sciences Publications Ltd), 2016-09 , Vol. 5 , N. e17092 , P. 1-50
- Notes :
- application/pdf, English
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1248915043
- Document Type :
- Electronic Resource
- Full Text :
- https://doi.org/10.7554.eLife.17092