Dataset Information

Protein sequences bound to mineral surfaces persist into deep time.

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 the palaeontological 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 ~16 Ma at a constant 10°C).

SUBMITTER: Demarchi B

PROVIDER: S-EPMC5039028 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Protein sequences bound to mineral surfaces persist into deep time.

Demarchi Beatrice B Hall Shaun S Roncal-Herrero Teresa T Freeman Colin L CL Woolley Jos J Crisp Molly K MK Wilson Julie J Fotakis Anna A Fischer Roman R Kessler Benedikt M BM Rakownikow Jersie-Christensen Rosa R Olsen Jesper V JV Haile James J Thomas Jessica J Marean Curtis W CW Parkington John J Presslee Samantha S Lee-Thorp Julia J Ditchfield Peter P Hamilton Jacqueline F JF Ward Martyn W MW Wang Chunting Michelle CM Shaw Marvin D MD Harrison Terry T Domínguez-Rodrigo Manuel M MacPhee Ross DE R Kwekason Amandus A Ecker Michaela M Kolska Horwitz Liora L Chazan Michael M Kröger Roland R Thomas-Oates Jane J Harding John H JH Cappellini Enrico E Penkman Kirsty K Collins Matthew J MJ

eLife 20160927

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 the palaeontological 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. Molecu ...[more]

PMID: 27668515

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Project description:Motivation:Protein fold recognition is an important problem in structural bioinformatics. Almost all traditional fold recognition methods use sequence (homology) comparison to indirectly predict the fold of a target protein based on the fold of a template protein with known structure, which cannot explain the relationship between sequence and fold. Only a few methods had been developed to classify protein sequences into a small number of folds due to methodological limitations, which are not generally useful in practice. Results:We develop a deep 1D-convolution neural network (DeepSF) to directly classify any protein sequence into one of 1195 known folds, which is useful for both fold recognition and the study of sequence-structure relationship. Different from traditional sequence alignment (comparison) based methods, our method automatically extracts fold-related features from a protein sequence of any length and maps it to the fold space. We train and test our method on the datasets curated from SCOP1.75, yielding an average classification accuracy of 75.3%. On the independent testing dataset curated from SCOP2.06, the classification accuracy is 73.0%. We compare our method with a top profile-profile alignment method-HHSearch on hard template-based and template-free modeling targets of CASP9-12 in terms of fold recognition accuracy. The accuracy of our method is 12.63-26.32% higher than HHSearch on template-free modeling targets and 3.39-17.09% higher on hard template-based modeling targets for top 1, 5 and 10 predicted folds. The hidden features extracted from sequence by our method is robust against sequence mutation, insertion, deletion and truncation, and can be used for other protein pattern recognition problems such as protein clustering, comparison and ranking. Availability and implementation:The DeepSF server is publicly available at: http://iris.rnet.missouri.edu/DeepSF/. Contact:chengji@missouri.edu. Supplementary information:Supplementary data are available at Bioinformatics online.

Project description:ObjectivesTo generate pseudo-CT (pCT) images of the pelvis from zero echo time (ZTE) MR sequences and compare them to conventional CT.MethodsNinety-one patients were prospectively scanned with CT and MRI including ZTE sequences of the pelvis. Eleven ZTE image volumes were excluded due to implants and severe B1 field inhomogeneity. Out of the 80 data sets, 60 were used to train and update a deep learning (DL) model for pCT image synthesis from ZTE sequences while the remaining 20 cases were selected as an evaluation cohort. CT and pCT images were assessed qualitatively and quantitatively by two readers.ResultsMean pCT ratings of qualitative parameters were good to perfect (2-3 on a 4-point scale). Overall intermodality agreement between CT and pCT was good (ICC = 0.88 (95% CI: 0.85-0.90); p < 0.001) with excellent interreader agreements for pCT (ICC = 0.91 (95% CI: 0.88-0.93); p < 0.001). Most geometrical measurements did not show any significant difference between CT and pCT measurements (p > 0.05) with the exception of transverse pelvic diameter measurements and lateral center-edge angle measurements (p = 0.001 and p = 0.002, respectively). Image quality and tissue differentiation in CT and pCT were similar without significant differences between CT and pCT CNRs (all p > 0.05).ConclusionsUsing a DL-based algorithm, it is possible to synthesize pCT images of the pelvis from ZTE sequences. The pCT images showed high bone depiction quality and accurate geometrical measurements compared to conventional CT. CRITICAL RELEVANCE STATEMENT: pCT images generated from MR sequences allow for high accuracy in evaluating bone without the need for radiation exposure. Radiological applications are broad and include assessment of inflammatory and degenerative bone disease or preoperative planning studies.Key pointspCT, based on DL-reconstructed ZTE MR images, may be comparable with true CT images. Overall, the intermodality agreement between CT and pCT was good with excellent interreader agreements for pCT. Geometrical measurements and tissue differentiation were similar in CT and pCT images.

Dataset Information

Protein sequences bound to mineral surfaces persist into deep time.

Publications

Protein sequences bound to mineral surfaces persist into deep time.

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