6533b873fe1ef96bd12d564f
RESEARCH PRODUCT
Shell proteome of rhynchonelliform brachiopods.
Danièle GaspardFrédéric MarinMaggie CusackArul MarieFrançoise ImmelNathalie Guichardsubject
BiomineralizationProteomicsProteomeShell (structure)BrachiopodsBiologyMatrix (biology)ProteomicsCalcium CarbonatePaleontologychemistry.chemical_compoundCalcification PhysiologicAnimal ShellsStructural Biology[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ShellAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsCalciteMineralsPhylumMarine invertebratesExtracellular matrix[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsInvertebrateschemistryEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomePeptidesBiomineralizationdescription
7 pages; International audience; Brachiopods are a phylum of marine invertebrates that have an external bivalved shell to protect their living tissues. With few exceptions, this biomineralized structure is composed of calcite, mixed together with a minor organic fraction, comprising secreted proteins that become occluded in the shell structure, once formed. This organic matrix is thought to display several functions, in particular, to control mineral deposition and to regulate crystallite shapes. Thus, identifying the primary structure of matrix proteins is a prerequisite for generating bioinspired materials with tailored properties. In this study, we employed a proteomic approach to identify numerous peptides that constitute the shell proteins, in three rhynchonellid brachiopods from different localities. Our results suggest that the shell protein repertoires identified thus far, differ from that of better known calcifying metazoans, such as molluscs.
year | journal | country | edition | language |
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2015-06-01 |