6533b855fe1ef96bd12b0aca

RESEARCH PRODUCT

Skeletal organic matrices in molluscs: origin, evolution, diagenesis

Christophe DurletFrédéric MarinTakeshi TakeuchiElias SamankassouDavorin MedakovicAurélien ChmielIrina Bundeleva

subject

0301 basic medicineProteomicsSubfossilProteinBiologyFunctional domainsProteomicsbiology.organism_classificationFossilizationSequencesTridacnaDiagenesisDiagenesis[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]03 medical and health sciences030104 developmental biology0302 clinical medicineOrder (biology)Evolutionary biologyMollusc shellShellIdentification (biology)14. Life underwaterMollusc030217 neurology & neurosurgery

description

8 pages; International audience; The mollusc shell comprises a small amount of organic macromolecules, mostly proteins and polysaccharides, which, all together, constitute the skeletal organic matrix (SOM). In the recent years, the study of the SOM of about two dozens of mollusc species via transcriptomics and/or proteomics has led to the identification of hundreds of shell-associated proteins. This rapidly growing set of data allows several comparisons, shedding light on similarities and differences at the primary structure level and on some peculiar evolutionary mechanisms that may have affected SOM proteins. In addition, it constitutes a prerequisite for investigating the SOM repertoires of sub-fossils or fossil specimens, closely related to known extant species, in order to revisit diagenetic processes, i.e. how SOM proteins degrade during fossilization. These two aspects are briefly exemplified here: on the one hand, Aplysia californica, the sea hare, exhibits a vestigial internal shell that has kept a proteomic signature similar to that found in fully functional external shells. On the other hand, subfossil specimens of the giant clam Tridacna, collected in French Polynesia, precisely dated and analysed by proteomics for their SOM content, comprise several preserved proteins that can still be identified by their peptide signature, in spite of information losses likely due to diagenetic transformations.

10.1007/978-981-13-1002-7_34https://hal.archives-ouvertes.fr/hal-01895413/document