Collagen sequence analysis of fossil camels, Camelops and c.f. Paracamelus, from the Arctic and sub-Arctic of Plio-Pleistocene North America.

@article{Buckley2019CollagenSA,
  title={Collagen sequence analysis of fossil camels, Camelops and c.f. Paracamelus, from the Arctic and sub-Arctic of Plio-Pleistocene North America.},
  author={Michael Buckley and Craig Lawless and Natalia Rybczynski},
  journal={Journal of proteomics},
  year={2019},
  volume={194},
  pages={
          218-225
        }
}

Figures and Tables from this paper

Description of a fossil camelid from the Pleistocene of Argentina, and a cladistic analysis of the Camelinae

A divergence between Lamini and Camelini predating the Barstovian (16 Mya) is indicated, and Camelops appears as monophyletic within the Camelini.

Extinct species identification from Upper Pleistocene bone fragments not identifiable from their osteomorphological studies by proteomics analysis

Proteomics successfully identified the bovidae and ursidae families providing new information to the paleontologists on these objects, and one retoucher was identified to be potentially from the Ursus spelaeus species.

Meta-proteomic analysis of two mammoth’s trunks by EVA technology and high-resolution mass spectrometry for an indirect picture of their habitat and the characterization of the collagen type I, alpha-1 and alpha-2 sequence

The present work reports the results of the metaproteomic analysis performed on the middle part of a trunk, and on the portion of an trunk tip tissue of two different woolly mammoths some 30,000 years old, which yielded an indirect description of the habitat of these two mammoths and an improved characterization of the collagen type I, alpha-1 and alpha-2 chains.

Palaeoproteomic analysis of Pleistocene cave hyenas from east Asia

This marks the first proteomic data generated from cave hyenas, adding new molecular data to the east Asian populations of Crocuta, and reveals two different groups of cave Hyenas in east Asia.

Deep Time Paleoproteomics: Looking Forward.

The history and current state of deep time paleoproteomics (DTPp), here defined as Paleoproteomic study of samples ∼1 million years (1 Ma) or more in age, is discussed and the future of DTPp research is discussed, including what the authors see as critical ways the field can expand, advancements in technology that can be utilized, and the types of questions DTPP can address.

Paleoproteomics

Looking to the future, innovative solutions and emerging technology will play an important role in enabling us to access the still unexplored “dark” proteome, allowing for a fuller understanding of the role ancient proteins can play in the interpretation of the past.

Exceptional preservation of nonmineralized biomaterials in Cenozoic fossils of the Mammalia clade

The members of the Mammalia class experienced high ecological, morphological and taxonomic diversification during the Cenozoic Era. With technological advances in molecular paleontology in recent

References

SHOWING 1-10 OF 44 REFERENCES

Genomic Data from Extinct North American Camelops Revise Camel Evolutionary History.

It is found that Camelops is sister to African and Asian bactrian and dromedary camels, to the exclusion of South American camelids (llamas, guanacos, alpacas, and vicuñas).

Collagen Sequence Analysis of the Extinct Giant Ground Sloths Lestodon and Megatherium

Examination of phylogenetic potential of proteomics-based sequencing through the analysis of collagen extracted from two extinct giant ground sloths, Lestodon and Megatherium highlights that proteomics methods could yield plausible phylogenies that share similarities with other methods, but have the potential to be more useful in fossils beyond the limits of ancient DNA survival.

Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen*

Bone samples from several vertebrates collected from the Ziegler Reservoir fossil site, in Snowmass Village, Colorado, and processed for proteomics analysis resulted in extensive fibrillar collagen sequence coverage, including the identification of posttranslational modifications of collagen.

Ancient collagen reveals evolutionary history of the endemic South American ‘ungulates’

  • M. Buckley
  • Biology
    Proceedings of the Royal Society B: Biological Sciences
  • 2015
A molecular phylogeny for both Macrauchenia patachonica (Litopterna) and Toxodon platensis (Notoungulata) recovered using proteomics-based (liquid chromatography–tandem mass spectrometry) sequencing analyses of bone collagen is presented, placing both taxa in a clade that is monophyletic with the perissodactyls, which today are represented by horses, rhinoceroses and tapirs.

A fossil protein chimera; difficulties in discriminating dinosaur peptide sequences from modern cross-contamination

Collagen is extracted from bone samples of three individuals of ostrich to imply that cross-contamination cannot be ruled out, and that appropriate measures to test for endogeneity should be further evaluated.

A Molecular Phylogeny of Plesiorycteropus Reassigns the Extinct Mammalian Order ‘Bibymalagasia’

The first known molecular sequence data for Plesiorycteropus is presented, obtained from the bone protein collagen (I), which places the ‘Malagasy aardvark’ as more closely related to tenrecs than aardVarks, suggesting that the taxonomic order ‘Bibymalagasia’ is obsolete.

Biomolecular Characterization and Protein Sequences of the Campanian Hadrosaur B. canadensis

Microstructural and immunological data are consistent with preservation of multiple bone matrix and vessel proteins, and phylogenetic analyses of Brachylophosaurus collagen sequenced by mass spectrometry robustly support the bird-dinosaur clade, consistent with an endogenous source for these collagen peptides.

Protein Sequences from Mastodon and Tyrannosaurus Rex Revealed by Mass Spectrometry

The presence of T. rex sequences indicates that their peptide bonds were remarkably stable, and mass spectrometry can be used to determine unique sequences from ancient organisms from peptide fragmentation patterns, a valuable tool to study the evolution and adaptation of ancient taxa from which genomic sequences are unlikely to be obtained.

Collagen survival and its use for species identification in Holocene-lower Pleistocene bone fragment

A systematic investigation of amino acid composition and collagen peptide mass fingerprints (PMF) for a range of samples dating back approximately 1.5 million years extends the range for collagen sequencing to the Lower Pleistocene as confirmed by the presence of collagen peptides in bones from the Weybourne Crag.