Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins.
peer reviewed We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun sequence ancient protein remains extracted from a 43 000 year old woolly mammoth ( Mammuthus primigenius ) bone preserved in the Siberian permafrost. For the first time, 126 unique protein accessions, mostly...
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Online Access: | https://orbilu.uni.lu/handle/10993/26349 https://doi.org/10.1021/pr200721u |
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ftunivluxembourg:oai:orbilu.uni.lu:10993/26349 2024-04-21T08:10:16+00:00 Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. Cappellini, Enrico Jensen, Lars J. Szklarczyk, Damian Ginolhac, Aurélien da Fonseca, Rute A. R. Stafford, Thomas W. Holen, Steven R. Collins, Matthew J. Orlando, Ludovic Willerslev, Eske Gilbert, M. Thomas P. Olsen, Jesper V. 2012 https://orbilu.uni.lu/handle/10993/26349 https://doi.org/10.1021/pr200721u en eng American Chemical Society urn:issn:1535-3907 https://orbilu.uni.lu/handle/10993/26349 info:hdl:10993/26349 doi:10.1021/pr200721u scopus-id:2-s2.0-84856667924 info:pmid:22103443 wos:000300458300035 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess Journal of Proteome Research, 11 (2), 917-26 (2012) Amino Acid Sequence Amino Acid Substitution Animals Elephants Femur/chemistry Fossils Mammoths/metabolism Molecular Sequence Data Proteins/chemistry/classification Proteome/analysis/chemistry Proteomics/methods Sequence Analysis Protein Serum Albumin/chemistry Siberia Tandem Mass Spectrometry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2012 ftunivluxembourg https://doi.org/10.1021/pr200721u 2024-03-27T14:11:08Z peer reviewed We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun sequence ancient protein remains extracted from a 43 000 year old woolly mammoth ( Mammuthus primigenius ) bone preserved in the Siberian permafrost. For the first time, 126 unique protein accessions, mostly low-abundance extracellular matrix and plasma proteins, were confidently identified by solid molecular evidence. Among the best characterized was the carrier protein serum albumin, presenting two single amino acid substitutions compared to extant African ( Loxodonta africana ) and Indian ( Elephas maximus ) elephants. Strong evidence was observed of amino acid modifications due to post-mortem hydrolytic and oxidative damage. A consistent subset of this permafrost bone proteome was also identified in more recent Columbian mammoth ( Mammuthus columbi ) samples from temperate latitudes, extending the potential of the approach described beyond subpolar environments. Mass spectrometry-based ancient protein sequencing offers new perspectives for future molecular phylogenetic inference and physiological studies on samples not amenable to ancient DNA investigation. This approach therefore represents a further step into the ongoing integration of different high-throughput technologies for identification of ancient biomolecules, unleashing the field of paleoproteomics. Article in Journal/Newspaper permafrost Siberia University of Luxembourg: ORBilu - Open Repository and Bibliography Journal of Proteome Research 11 2 917 926 |
institution |
Open Polar |
collection |
University of Luxembourg: ORBilu - Open Repository and Bibliography |
op_collection_id |
ftunivluxembourg |
language |
English |
topic |
Amino Acid Sequence Amino Acid Substitution Animals Elephants Femur/chemistry Fossils Mammoths/metabolism Molecular Sequence Data Proteins/chemistry/classification Proteome/analysis/chemistry Proteomics/methods Sequence Analysis Protein Serum Albumin/chemistry Siberia Tandem Mass Spectrometry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Amino Acid Sequence Amino Acid Substitution Animals Elephants Femur/chemistry Fossils Mammoths/metabolism Molecular Sequence Data Proteins/chemistry/classification Proteome/analysis/chemistry Proteomics/methods Sequence Analysis Protein Serum Albumin/chemistry Siberia Tandem Mass Spectrometry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Cappellini, Enrico Jensen, Lars J. Szklarczyk, Damian Ginolhac, Aurélien da Fonseca, Rute A. R. Stafford, Thomas W. Holen, Steven R. Collins, Matthew J. Orlando, Ludovic Willerslev, Eske Gilbert, M. Thomas P. Olsen, Jesper V. Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
topic_facet |
Amino Acid Sequence Amino Acid Substitution Animals Elephants Femur/chemistry Fossils Mammoths/metabolism Molecular Sequence Data Proteins/chemistry/classification Proteome/analysis/chemistry Proteomics/methods Sequence Analysis Protein Serum Albumin/chemistry Siberia Tandem Mass Spectrometry Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun sequence ancient protein remains extracted from a 43 000 year old woolly mammoth ( Mammuthus primigenius ) bone preserved in the Siberian permafrost. For the first time, 126 unique protein accessions, mostly low-abundance extracellular matrix and plasma proteins, were confidently identified by solid molecular evidence. Among the best characterized was the carrier protein serum albumin, presenting two single amino acid substitutions compared to extant African ( Loxodonta africana ) and Indian ( Elephas maximus ) elephants. Strong evidence was observed of amino acid modifications due to post-mortem hydrolytic and oxidative damage. A consistent subset of this permafrost bone proteome was also identified in more recent Columbian mammoth ( Mammuthus columbi ) samples from temperate latitudes, extending the potential of the approach described beyond subpolar environments. Mass spectrometry-based ancient protein sequencing offers new perspectives for future molecular phylogenetic inference and physiological studies on samples not amenable to ancient DNA investigation. This approach therefore represents a further step into the ongoing integration of different high-throughput technologies for identification of ancient biomolecules, unleashing the field of paleoproteomics. |
format |
Article in Journal/Newspaper |
author |
Cappellini, Enrico Jensen, Lars J. Szklarczyk, Damian Ginolhac, Aurélien da Fonseca, Rute A. R. Stafford, Thomas W. Holen, Steven R. Collins, Matthew J. Orlando, Ludovic Willerslev, Eske Gilbert, M. Thomas P. Olsen, Jesper V. |
author_facet |
Cappellini, Enrico Jensen, Lars J. Szklarczyk, Damian Ginolhac, Aurélien da Fonseca, Rute A. R. Stafford, Thomas W. Holen, Steven R. Collins, Matthew J. Orlando, Ludovic Willerslev, Eske Gilbert, M. Thomas P. Olsen, Jesper V. |
author_sort |
Cappellini, Enrico |
title |
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
title_short |
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
title_full |
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
title_fullStr |
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
title_full_unstemmed |
Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
title_sort |
proteomic analysis of a pleistocene mammoth femur reveals more than one hundred ancient bone proteins. |
publisher |
American Chemical Society |
publishDate |
2012 |
url |
https://orbilu.uni.lu/handle/10993/26349 https://doi.org/10.1021/pr200721u |
genre |
permafrost Siberia |
genre_facet |
permafrost Siberia |
op_source |
Journal of Proteome Research, 11 (2), 917-26 (2012) |
op_relation |
urn:issn:1535-3907 https://orbilu.uni.lu/handle/10993/26349 info:hdl:10993/26349 doi:10.1021/pr200721u scopus-id:2-s2.0-84856667924 info:pmid:22103443 wos:000300458300035 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1021/pr200721u |
container_title |
Journal of Proteome Research |
container_volume |
11 |
container_issue |
2 |
container_start_page |
917 |
op_container_end_page |
926 |
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1796951663168192512 |