FN Archimer Export Format
PT J
TI Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization
BT 
AF JOUBERT, Caroline
   PIQUEMAL, David
   MARIE, Benjamin
   MANCHON, Laurent
   PIERRAT, Fabien
   ZANELLA-CLEON, Isabelle
   COCHENNEC-LAUREAU, Nathalie
   GUEGUEN, Yannick
   MONTAGNANI, Caroline
AS 1:1;2:2;3:3;4:2;5:2;6:4;7:5;8:1;9:1;
FF 1:;2:;3:;4:;5:;6:;7:PDG-DPCP;8:PDG-DOP-DCOP-AQUAPOL-LBQP;9:PDG-DOP-DCM-BOME-LALR;
C1 IFREMER, Lab Biotechnol & Qual Perle, Ctr Oceanol Pacifique, Taravao 98719, Fr Polynesia.
   Skuldtech, F-34090 Montpellier, France.
   Univ Bourgogne, UMR CNRS Biogeosci 5561, F-21000 Dijon, France.
   Univ Lyon 1, IFR BioSci Gerland Lyon Sud 128, UMR CNRS 5086, IBCP, F-69367 Lyon, France.
   IFREMER, Ctr Nantes, F-44311 Nantes 03, France.
C2 IFREMER, FRANCE
   SKULDTECH, FRANCE
   UNIV BOURGOGNE, FRANCE
   UNIV LYON, FRANCE
   IFREMER, FRANCE
SI TAHITI
   NANTES
   MONTPELLIER
SE PDG-DOP-DCOP-AQUAPOL-LBQP
   PDG-DPCP
   PDG-DOP-DCM-BOME-LALR
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 4.206
TC 179
UR https://archimer.ifremer.fr/doc/00020/13154/10202.pdf
LA English
DT Article
AB Background: The shell of the pearl-producing bivalve Pinctada margaritifera is composed of an organic cell-free matrix that plays a key role in the dynamic process of biologically-controlled biomineralization. In order to increase genomic resources and identify shell matrix proteins implicated in biomineralization in P. margaritifera, high-throughput Expressed Sequence Tag (EST) pyrosequencing was undertaken on the calcifying mantle, combined with a proteomic analysis of the shell. Results: We report the functional analysis of 276 738 sequences, leading to the constitution of an unprecedented catalog of 82 P. margaritifera biomineralization-related mantle protein sequences. Components of the current "chitin-silk fibroin gel-acidic macromolecule" model of biomineralization processes were found, in particular a homolog of a biomineralization protein (Pif-177) recently discovered in P. fucata. Among these sequences, we could show the localization of two other biomineralization protein transcripts, pmarg-aspein and pmarg-pearlin, in two distinct areas of the outer mantle epithelium, suggesting their implication in calcite and aragonite formation. Finally, by combining the EST approach with a proteomic mass spectrometry analysis of proteins isolated from the P. margaritifera shell organic matrix, we demonstrated the presence of 30 sequences containing almost all of the shell proteins that have been previously described from shell matrix protein analyses of the Pinctada genus. The integration of these two methods allowed the global composition of biomineralizing tissue and calcified structures to be examined in tandem for the first time. Conclusions: This EST study made on the calcifying tissue of P. margaritifera is the first description of pyrosequencing on a pearl-producing bivalve species. Our results provide direct evidence that our EST data set covers most of the diversity of the matrix protein of P. margaritifera shell, but also that the mantle transcripts encode proteins present in P. margaritifera shell, hence demonstrating their implication in shell formation. Combining transcriptomic and proteomic approaches is therefore a powerful way to identify proteins involved in biomineralization. Data generated in this study supply the most comprehensive list of biomineralization-related sequences presently available among protostomian species, and represent a major breakthrough in the field of molluskan biomineralization.
PY 2010
PD NOV
SO Bmc Genomics
SN 1471-2164
PU Biomed Central Ltd
VL 11
UT 000284412500001
BP 1
EP 13
DI 10.1186/1471-2164-11-613
ID 13154
ER

EF