scholarly journals PU14, a Novel Matrix Protein, Participates in Pearl Oyster, Pinctada Fucata, Shell Formation

2021 ◽  
Author(s):  
Yinghui Ji ◽  
Xue Yang ◽  
Dong Yang ◽  
Rongqing Zhang
Keyword(s):  
Matrix Protein ◽  
Pinctada Fucata ◽  
Matrix Proteins ◽  
In Vitro Experiments ◽  
Shell Formation ◽  
Prismatic Layer ◽  
Shell Matrix ◽  
Shell Matrix Proteins ◽  
Functional Analyses

AbstractBiomineralization is a widespread biological process, involved in the formation of shells, teeth, and bones. Shell matrix proteins have been widely studied for their importance during shell formation. In 2015, our group identified 72 unique shell matrix proteins in Pinctada fucata, among which PU14 is a matrix protein detected in the soluble fraction that solely exists in the prismatic layer. However, the function of PU14 is still unclear. In this study, the full-length cDNA sequence of PU14 was obtained and functional analyses of PU14 protein during shell formation were performed. The deduced protein has a molecular mass of 77.8 kDa and an isoelectric point of 11.34. The primary protein structure contains Gln-rich and random repeat units, which are typical characteristics of matrix protein and indicate its potential function during shell formation. In vivo and in vitro experiments indicated PU14 has prismatic layer functions during shell formation. The tissue expression patterns showed that PU14 was mainly expressed in the mantle tissue, which is consistent with prismatic layer formation. Notching experiments suggested that PU14 responded to repair and regenerate the injured shell. After inhibiting gene expression by injecting PU14-specific double-stranded RNA, the inner surface of the prismatic layer changed significantly and became rougher. Further, in vitro experiments showed that recombinant protein rPU14 impacted calcite crystal morphology. Taken together, characterization and functional analyses of a novel matrix protein, PU14, provide new insights about basic matrix proteins and their functions during shell formation.

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 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 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.

Cloning, characterization, and functional analysis of chitinase-like protein 1 in the shell of Pinctada fucata

2020 ◽  
Vol 52 (9) ◽  
pp. 954-966
Author(s):  
Yunpin Zhou ◽  
Yi Yan ◽  
Dong Yang ◽  
Guilan Zheng ◽  
Liping Xie ◽  
...  
Keyword(s):  
Pinctada Fucata ◽  
Negative Regulator ◽  
Matrix Proteins ◽  
Nacreous Layer ◽  
Shell Formation ◽  
Microscopy Imaging ◽  
Polymerase Chain ◽  
First Time

Abstract Biomineralization, especially shell formation, is a sophisticated process regulated by various matrix proteins. Pinctada fucata chitinase-like protein 1 (Pf-Clp1), which belongs to the GH18 family, was discovered by our group using in-depth proteomic analysis. However, its function is still unclear. In this study, we first obtained the full-length cDNA sequence of Pf-Clp1 by RACE. Real-time polymerase chain reaction results revealed that Pf-Clp1 was highly expressed in the important biomineralization tissues, the mantle edge and the mantle pallial. We expressed and purified recombinant protein rPf-Clp1 in vitro to investigate the function of Pf-Clp1 on CaCO3 crystallization. Scanning electron microscopy imaging and Raman spectroscopy revealed that rPf-Clp1 was able to affect the morphologies of calcite crystal in vitro. Shell notching experiments suggested that Pf-Clp1 might function as a negative regulator during shell formation in vivo. Knockdown of Pf-Clp1 by RNAi led to the overgrowth of aragonite tablets, further confirming its potential negative regulation on biomineralization, especially in the nacreous layer. Our work revealed the potential function of molluscan Clp in shell biomineralization for the first time and unveiled some new understandings toward the molecular mechanism of shell formation.

scholarly journals Phylogenetic comparisons reveal mosaic histories of larval and adult shell matrix protein deployment in pteriomorph bivalves

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ran Zhao ◽  
Takeshi Takeuchi ◽  
Ryo Koyanagi ◽  
Alejandro Villar-Briones ◽  
Lixy Yamada ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Phylogenetic Analyses ◽  
Organic Matrix ◽  
Pinctada Fucata ◽  
Chitin Binding Domain ◽  
Shell Matrix ◽  
Shell Matrix Protein ◽  
Shell Matrix Proteins ◽  
Factor Type ◽  
Von Willebrand

AbstractMolluscan shells are organo-mineral composites, in which the dominant calcium carbonate is intimately associated with an organic matrix comprised mainly of proteins and polysaccharides. However, whether the various shell matrix proteins (SMPs) date to the origin of hard skeletons in the Cambrian, or whether they represent later deployment through adaptive evolution, is still debated. In order to address this issue and to better understand the origins and evolution of biomineralization, phylogenetic analyses have been performed on the three SMP families, Von Willebrand factor type A (VWA) and chitin-binding domain-containing protein (VWA-CB dcp), chitobiase, and carbonic anhydrase (CA), which exist in both larval and adult shell proteomes in the bivalves, Crassostrea gigas and Pinctada fucata. In VWA-CB dcp and chitobiase, paralogs for larval and adult SMPs evolved before the divergence of these species. CA-SMPs have been taken as evidence for ancient origins of SMPs by their presumed indispensable function in biomineralization and ubiquitous distribution in molluscs. However, our results indicate gene duplications that gave rise to separate deployments as larval and adult CA-SMPs occurred independently in each lineage after their divergence, which is considerably more recent than hitherto assumed, supporting the “recent heritage and fast evolution” scenario for SMP evolution.

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