FN Archimer Export Format
PT J
TI Characterization of MRNP34, a novel methionine-rich nacre protein from the pearl oysters
BT 
AF MARIE, Benjamin
   JOUBERT, Caroline
   BELLIARD, Corinne
   TAYALE, Alexandre
   ZANELLA-CLEON, Isabelle
   MARIN, Frederic
   GUEGUEN, Yannick
   MONTAGNANI, Caroline
AS 1:;2:;3:;4:;5:;6:;7:;8:;
FF 1:;2:PDG-RBE-RMPF-EP;3:PDG-RBE-RMPF-EP;4:PDG-RBE-RMPF-EP;5:;6:;7:PDG-RBE-RMPF-EP;8:PDG-RBE-BOME-LALR;
C1 IFREMER, Ctr Oceanolog Pacifique, LBQP, Taravao, Fr Polynesia.
   Univ Bourgogne, CNRS, UMR 5561, Dijon, France.
   Univ Lyon 1, CNRS, IBCP, IFR BioSci 128,UMR 5086, F-69365 Lyon, France.
C2 IFREMER, FRANCE
   UNIV BOURGOGNE, FRANCE
   UNIV LYON, FRANCE
SI TAHITI
   MONTPELLIER
SE PDG-RBE-RMPF-EP
   PDG-RBE-BOME-LALR
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 3.91
TC 23
UR https://archimer.ifremer.fr/doc/00077/18870/16645.pdf
LA English
DT Article
DE ;Matrix protein;Methionine-rich;Biomineralization;Mollusc;Nacre;Calcifying mantle
AB Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO3 and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those of the other nacre proteins already described. This unusual methionine-rich protein is a new member in the growing list of low complexity domain containing proteins that are associated with biocalcifications. These observations offer new insights to the molecular mechanisms of biomineralization.
PY 2012
PD MAY
SO Amino Acids
SN 0939-4451
PU Springer
VL 42
IS 5
UT 000302812700045
BP 2009
EP 2017
DI 10.1007/s00726-011-0932-0
ID 18870
ER

EF