Analysis of low complex region peptides derived from mollusk shell matrix proteins using CID, high-energy collisional dissociation, and electron transfer dissociation on an LTQ-orbitrap: Implications for peptide to spectrum match

PROTEOMICS ◽  
2012 ◽  
Vol 12 (19-20) ◽  
pp. 3069-3075 ◽  
Author(s):  
Arul Marie ◽  
Sandra Alves ◽  
Benjamin Marie ◽  
Lionel Dubost ◽  
Laurent Bédouet ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electron Transfer Dissociation ◽  
High Energy ◽  
Matrix Proteins ◽  
Complex Region ◽  
Shell Matrix ◽  
Shell Matrix Proteins ◽  
Low Complex ◽  
Mollusk Shell

scholarly journals Shell matrix proteins of the clam, Mya truncata: Roles beyond shell formation through proteomic study

2016 ◽  
Vol 27 ◽  
pp. 69-74 ◽  
Author(s):  
Jaison Arivalagan ◽  
Benjamin Marie ◽  
Victoria A. Sleight ◽  
Melody S. Clark ◽  
Sophie Berland ◽  
...  
Keyword(s):  
Matrix Proteins ◽  
Shell Formation ◽  
Shell Matrix ◽  
Proteomic Study ◽  
Shell Matrix Proteins

scholarly journals The role of phosphorylation and dephosphorylation of shell matrix proteins in shell formation: an in vivo and in vitro study

CrystEngComm ◽  
2018 ◽  
Vol 20 (27) ◽  
pp. 3905-3916 ◽  
Author(s):  
Jinzhe Du ◽  
Guangrui Xu ◽  
Chuang Liu ◽  
Rongqing Zhang
Keyword(s):  
Calcium Carbonate ◽  
In Vitro Study ◽  
Matrix Proteins ◽  
Shell Formation ◽  
Carbonate Formation ◽  
Shell Matrix ◽  
Shell Matrix Proteins

Phosphorylation of shell matrix proteins is critical for shell formation in vivo and can modulate calcium carbonate formation in vitro.

scholarly journals In-depth proteomic analysis of shell matrix proteins of Pinctada fucata

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Chuang Liu ◽  
Shiguo Li ◽  
Jingjing Kong ◽  
Yangjia Liu ◽  
Tianpeng Wang ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Pinctada Fucata ◽  
Matrix Proteins ◽  
Shell Matrix ◽  
Shell Matrix Proteins

scholarly journals The ‘Shellome’ of the Crocus Clam Tridacna crocea Emphasizes Essential Components of Mollusk Shell Biomineralization

2021 ◽  
Vol 12 ◽  
Author(s):  
Takeshi Takeuchi ◽  
Manabu Fujie ◽  
Ryo Koyanagi ◽  
Laurent Plasseraud ◽  
Isabelle Ziegler-Devin ◽  
...  
Keyword(s):  
Organic Matrix ◽  
The Other ◽  
Matrix Proteins ◽  
Shell Formation ◽  
Molluscan Shell ◽  
Shell Matrix ◽  
Essential Components ◽  
Shell Matrix Proteins ◽  
Shell Organic Matrix ◽  
Tridacna Crocea

Molluscan shells are among the most fascinating research objects because of their diverse morphologies and textures. The formation of these delicate biomineralized structures is a matrix-mediated process. A question that arises is what are the essential components required to build these exoskeletons. In order to understand the molecular mechanisms of molluscan shell formation, it is crucial to identify organic macromolecules in different shells from diverse taxa. In the case of bivalves, however, taxon sampling in previous shell proteomics studies are focused predominantly on representatives of the class Pteriomorphia such as pearl oysters, edible oysters and mussels. In this study, we have characterized the shell organic matrix from the crocus clam, Tridacna crocea, (Heterodonta) using various biochemical techniques, including SDS-PAGE, FT-IR, monosaccharide analysis, and enzyme-linked lectin assay (ELLA). Furthermore, we have identified a number of shell matrix proteins (SMPs) using a comprehensive proteomics approach combined to RNA-seq. The biochemical studies confirmed the presence of proteins, polysaccharides, and sulfates in the T. crocea shell organic matrix. Proteomics analysis revealed that the majority of the T. crocea SMPs are novel and dissimilar to known SMPs identified from the other bivalve species. Meanwhile, the SMP repertoire of the crocus clam also includes proteins with conserved functional domains such as chitin-binding domain, VWA domain, and protease inhibitor domain. We also identified BMSP (Blue Mussel Shell Protein, originally reported from Mytilus), which is widely distributed among molluscan shell matrix proteins. Tridacna SMPs also include low-complexity regions (LCRs) that are absent in the other molluscan genomes, indicating that these genes may have evolved in specific lineage. These results highlight the diversity of the organic molecules – in particular proteins – that are essential for molluscan shell formation.

scholarly journals Shell matrix proteins - a potential tool for investigating the phylogenetic relationships of the Echinodermata

1992 ◽  
Vol 6 ◽  
pp. 236-236
Author(s):  
Emma S. Polson ◽  
J. Lawrence ◽  
L. L. Robbins
Keyword(s):  
Phylogenetic Relationships ◽  
Matrix Protein ◽  
Dna Analysis ◽  
Morphological Characters ◽  
Matrix Proteins ◽  
Molecular Weights ◽  
Shell Matrix ◽  
Shell Matrix Proteins ◽  
Luidia Clathrata ◽  
Mellita Tenuis

The phylogenetic relationships of the echinoderms remains controversial due to the traditional use of morphological characters which do not reflect convergent evolution. While biochemical techniques and DNA analysis may be used in addition to morphological characters for analysis of living echinoderms, these tools cannot be extended to fossils. Shell matrix proteins - of echinoderms may be trapped and preserved for millions of years in fossil genera.Analysis of shell matrix protein from Astropectin irregularis, Luidia clathrata and Mellita tenuis, reveal the presence of at least three major proteins of approximate molecular weights 230, 83 and 17 kDa common to all species. Astropectin irregularis showed four additional major bands of molecular weights 150, 90, 52 and 35 kDa along with at least 12 minor bands. Luidia clathrata showed five additional major bands of molecular weights 99, 60, 40, 24 and 21 kDa and at least 13 other minor bands. Mellita tenuis showed three additional bands of molecular weights 115, 96, and 24 kDa along with at least 4 minor bands.As the three common proteins have been found in both seastars (A. irregularis and L. clathrata) and echinoids (Mellita tenuis), further analysis of these shell matrix proteins may be used to elucidate phylogenetic relationships within the Echinodermata. In addition homoplasies may be identified and phylogenetically reassessed.

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