دورية أكاديمية
Protein sequences bound to mineral surfaces persist into deep time
| العنوان: | Protein sequences bound to mineral surfaces persist into deep time |
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| المؤلفون: | Demarchi, Beatrice, Hall, Shaun, Roncal-herrero, Teresa, Freeman, Colin L., Woolley, Jos, Crisp, Molly K., Wilson, Julie, Fotakis, Anna, Fischer, Roman, Kessler, Benedikt M., Jersie-christensens, Rosa Rakownikow, Olsen, Jesper V., Haile, James, Thomas, Jessica, Marean, Curtis W., Parkington, John, Presslee, Samantha, Lee-thorp, Julia, Ditchfield, Peter, Hamilton, Jacqueline F., Ward, Martyn W., Wang, Chunting Michelle, Shaw, Marvin D., Harrison, Terry, Dominguez-rodrigo, Manuel, Macphee, Ross De, Kwekason, Amandus, Ecker, Michaels, Horwitz, Liora Kolska, Chazan, Michael, Kröger, Roland, Thomas-oates, Jane, Harding, John H., Cappellini, Enrico, Penkman, Kirsty, Collins, Matthew J. |
| المصدر: | Elife (2050-084X) (Elife Sciences Publications Ltd), 2016-09 , Vol. 5 , N. e17092 , P. 1-50 |
| بيانات النشر: | Elife Sciences Publications Ltd |
| سنة النشر: | 2016 |
| المجموعة: | Ifremer (French Research Institute for Exploitation of the Sea): Archimer |
| الوصف: | 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). |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | info:eu-repo/grantAgreement/EC/FP7/310637/EU//SMILEY; https://archimer.ifremer.fr/doc/00421/53219/54825.pdfTest; https://archimer.ifremer.fr/doc/00421/53219/54827.pdfTest; https://archimer.ifremer.fr/doc/00421/53219/54829.pdfTest; https://archimer.ifremer.fr/doc/00421/53219/54830.pdfTest; https://archimer.ifremer.fr/doc/00421/53219/54832.xlsxTest; https://archimer.ifremer.fr/doc/00421/53219Test/ |
| DOI: | 10.7554/eLife.17092 |
| الإتاحة: | https://doi.org/10.7554/eLife.17092Test https://archimer.ifremer.fr/doc/00421/53219/54825.pdfTest https://archimer.ifremer.fr/doc/00421/53219/54827.pdfTest https://archimer.ifremer.fr/doc/00421/53219/54829.pdfTest https://archimer.ifremer.fr/doc/00421/53219/54830.pdfTest https://archimer.ifremer.fr/doc/00421/53219/54832.xlsxTest https://archimer.ifremer.fr/doc/00421/53219Test/ |
| حقوق: | Copyright Demarchi et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. ; info:eu-repo/semantics/openAccess ; restricted use |
| رقم الانضمام: | edsbas.CEB9ED77 |
| قاعدة البيانات: | BASE |
| DOI: | 10.7554/eLife.17092 |
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