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doi: 10.1371/journal.pone.0020381. Epub 2011 Jun 8.

Dinosaur peptides suggest mechanisms of protein survival

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Dinosaur peptides suggest mechanisms of protein survival

James D San Antonio et al. PLoS One.2011.

Abstract

Eleven collagen peptide sequences recovered from chemical extracts of dinosaur bones were mapped onto molecular models of the vertebrate collagen fibril derived from extant taxa. The dinosaur peptides localized to fibril regions protected by the close packing of collagen molecules, and contained few acidic amino acids. Four peptides mapped to collagen regions crucial for cell-collagen interactions and tissue development. Dinosaur peptides were not represented in more exposed parts of the collagen fibril or regions mediating intermolecular cross-linking. Thus functionally significant regions of collagen fibrils that are physically shielded within the fibril may be preferentially preserved in fossils. These results show empirically that structure-function relationships at the molecular level could contribute to selective preservation in fossilized vertebrate remains across geological time, suggest a 'preservation motif', and bolster current concepts linking collagen structure to biological function. This non-random distribution supports the hypothesis that the peptides are produced by the extinct organisms and suggests a chemical mechanism for survival.

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Conflict of interest statement

Competing Interests:The lead author is an employee of private industry, Orthovita, Inc. However, this is an academic study that the company is allowing to be researched and published, and with which they have no financial or proprietary interest. The last author, J. Orgel, is a Biochemistry Section Editor of PLOS ONE. This does not alter the authors' adherence to all the PLOS ONE policies on sharing data and materials.

Figures

Figure 1
Figure 1.Tyrannosaurus rex femur (MOR 1125) from which demineralized matrix (insets; bars, 20µm) and peptides were obtained.
Courtesy Museum of the Rockies.
Figure 2
Figure 2. The collagen fibril (A) is composed of triple-helical monomers that polymerize in an overlapping fashion (B), and are derived from proteolysis of the soluble procollagen precursor (C).
Fibrils appear as periodic banded structures by electron microscopy; one D-period (expanded two-dimensional view of 67 nm segment of microfibril, box) contains the complete collagen sequence from elements of five monomers and includes an overlap and gap zone; arrow, left border of overlap zone. Image of the X-ray diffraction-derived fibril subunit structure: the microfibril (D) shows aggregates of five triple-helical, rope-like monomers; magnified view shows triple helix containing three peptide chains (two α1 and one α2 chains) (E). Many thousands of microfibrils polymerize and cross-link to form cable-like collagen fibrils of vertebrates. Modified from original research .
Figure 3
Figure 3. Dinosaur peptide sequence positions were mapped on the two dimensional human collagen fibril D-period schematic33.
Figure 4
Figure 4. X-ray diffraction model of the rat collagen microfibrilin situ; Integrins, predominant cell-binding site; MMP, matrix metalloproteinase cleavage site; FN, fibronectin binding site; decoron, decorin proteoglycan core protein binding sites; putative cell and matrix interaction domains35.
See this image and copyright information in PMC

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References

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