A Bivalve Biomineralization Toolbox
Abstract Mollusc shells are a result of the deposition of crystalline and amorphous calcite catalyzed by enzymes and shell matrix proteins (SMP). Developing a detailed understanding of bivalve mollusc biomineralization pathways is complicated not only by the multiplicity of shell forms and microstru...
Published in: | Molecular Biology and Evolution |
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Oxford University Press (OUP)
2021
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Online Access: | http://dx.doi.org/10.1093/molbev/msab153 http://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msab153/39310566/msab153.pdf http://academic.oup.com/mbe/article-pdf/38/9/4043/39882203/msab153.pdf |
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croxfordunivpr:10.1093/molbev/msab153 2024-06-23T07:52:18+00:00 A Bivalve Biomineralization Toolbox Yarra, Tejaswi Blaxter, Mark Clark, Melody S True, John European Union Seventh Framework Programme REA 2021 http://dx.doi.org/10.1093/molbev/msab153 http://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msab153/39310566/msab153.pdf http://academic.oup.com/mbe/article-pdf/38/9/4043/39882203/msab153.pdf en eng Oxford University Press (OUP) http://creativecommons.org/licenses/by/4.0/ Molecular Biology and Evolution volume 38, issue 9, page 4043-4055 ISSN 1537-1719 journal-article 2021 croxfordunivpr https://doi.org/10.1093/molbev/msab153 2024-06-04T06:11:57Z Abstract Mollusc shells are a result of the deposition of crystalline and amorphous calcite catalyzed by enzymes and shell matrix proteins (SMP). Developing a detailed understanding of bivalve mollusc biomineralization pathways is complicated not only by the multiplicity of shell forms and microstructures in this class, but also by the evolution of associated proteins by domain co-option and domain shuffling. In spite of this, a minimal biomineralization toolbox comprising proteins and protein domains critical for shell production across species has been identified. Using a matched pair design to reduce experimental noise from inter-individual variation, combined with damage-repair experiments and a database of biomineralization SMPs derived from published works, proteins were identified that are likely to be involved in shell calcification. Eighteen new, shared proteins likely to be involved in the processes related to the calcification of shells were identified by the analysis of genes expressed during repair in Crassostrea gigas, Mytilus edulis, and Pecten maximus. Genes involved in ion transport were also identified as potentially involved in calcification either via the maintenance of cell acid–base balance or transport of critical ions to the extrapallial space, the site of shell assembly. These data expand the number of candidate biomineralization proteins in bivalve molluscs for future functional studies and define a minimal functional protein domain set required to produce solid microstructures from soluble calcium carbonate. This is important for understanding molluscan shell evolution, the likely impacts of environmental change on biomineralization processes, materials science, and biomimicry research. Article in Journal/Newspaper Crassostrea gigas Oxford University Press Molecular Biology and Evolution |
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Oxford University Press |
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croxfordunivpr |
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English |
description |
Abstract Mollusc shells are a result of the deposition of crystalline and amorphous calcite catalyzed by enzymes and shell matrix proteins (SMP). Developing a detailed understanding of bivalve mollusc biomineralization pathways is complicated not only by the multiplicity of shell forms and microstructures in this class, but also by the evolution of associated proteins by domain co-option and domain shuffling. In spite of this, a minimal biomineralization toolbox comprising proteins and protein domains critical for shell production across species has been identified. Using a matched pair design to reduce experimental noise from inter-individual variation, combined with damage-repair experiments and a database of biomineralization SMPs derived from published works, proteins were identified that are likely to be involved in shell calcification. Eighteen new, shared proteins likely to be involved in the processes related to the calcification of shells were identified by the analysis of genes expressed during repair in Crassostrea gigas, Mytilus edulis, and Pecten maximus. Genes involved in ion transport were also identified as potentially involved in calcification either via the maintenance of cell acid–base balance or transport of critical ions to the extrapallial space, the site of shell assembly. These data expand the number of candidate biomineralization proteins in bivalve molluscs for future functional studies and define a minimal functional protein domain set required to produce solid microstructures from soluble calcium carbonate. This is important for understanding molluscan shell evolution, the likely impacts of environmental change on biomineralization processes, materials science, and biomimicry research. |
author2 |
True, John European Union Seventh Framework Programme REA |
format |
Article in Journal/Newspaper |
author |
Yarra, Tejaswi Blaxter, Mark Clark, Melody S |
spellingShingle |
Yarra, Tejaswi Blaxter, Mark Clark, Melody S A Bivalve Biomineralization Toolbox |
author_facet |
Yarra, Tejaswi Blaxter, Mark Clark, Melody S |
author_sort |
Yarra, Tejaswi |
title |
A Bivalve Biomineralization Toolbox |
title_short |
A Bivalve Biomineralization Toolbox |
title_full |
A Bivalve Biomineralization Toolbox |
title_fullStr |
A Bivalve Biomineralization Toolbox |
title_full_unstemmed |
A Bivalve Biomineralization Toolbox |
title_sort |
bivalve biomineralization toolbox |
publisher |
Oxford University Press (OUP) |
publishDate |
2021 |
url |
http://dx.doi.org/10.1093/molbev/msab153 http://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msab153/39310566/msab153.pdf http://academic.oup.com/mbe/article-pdf/38/9/4043/39882203/msab153.pdf |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
Molecular Biology and Evolution volume 38, issue 9, page 4043-4055 ISSN 1537-1719 |
op_rights |
http://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1093/molbev/msab153 |
container_title |
Molecular Biology and Evolution |
_version_ |
1802643557372133376 |