Genetic structure and polymorphisms of the N16 gene in Pinctada fucata

Nogawa, Chihiro; Baba, Hiroko; Masaoka, Tetsuji; Aoki, Hideo; Samata, Tetsuro

doi:10.1016/j.gene.2012.03.066

Cited by 14 publications

(23 citation statements)

References 21 publications

(23 reference statements)

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“…9,13,14,18,19 To date, 23 polymorphic forms of this family have been identified, and all of these forms are transcribed and actively expressed in the pearl oyster. 10,13 Interestingly, homologues of the n16 family have also been identified in the mollusks Pinctada maxima (N14 family) 11 and Pinctada margaritifera (Pmarg pearlin family). 9,12 This proteomic overlap suggests that n16-related sequences are an essential element in the construction of the nacre layer framework gel.…”

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confidence: 99%

A Nacre Protein, n16.3, Self-Assembles To Form Protein Oligomers That Dimensionally Limit and Organize Mineral Deposits

et al. 2014

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The mollusk shell is a complex biological material that integrates mineral phases with organic macromolecular components such as proteins. The role of proteins in the formation of the nacre layer (aragonite mineral phase) is poorly understood, particularly with regard to the organization of mineral deposits within the protein extracellular matrix and the identification of which proteins are responsible for this task. We report new experiments that provide insight into the role of the framework nacre protein, n16.3 (Pinctada fucata), as an organizer or assembler of calcium carbonate mineral clusters. Using a combination of biophysical techniques, we find that recombinant n16.3 (r-n16.3) oligomerizes to form amorphous protein films and particles that possess regions of disorder and mobility. These supramolecular assemblies possess an intrinsically disordered C-terminal region (T64-W98) and reorganize in the presence of Ca(2+) ions to form clustered protein oligomers. This Ca(2+)-induced reorganization leads to alterations in the molecular environments of Trp residues, the majority of which reside in putative aggregation-prone cross-β strand regions. Potentiometric Ca(2+) titrations reveal that r-n16.3 does not significantly affect the formation of prenucleation clusters in solution, and this suggests a role for this protein in postnucleation mineralization events. This is verified in subsequent in vitro mineralization assays in which r-n16.3 demonstrates its ability to form gel-like protein phases that organize and cluster nanometer-sized single-crystal calcite relative to protein-deficient controls. We conclude that the n16 nacre framework proteome creates a protein gel matrix that organizes and dimensionally limits mineral deposits. This process is highly relevant to the formation of ordered, nanometer-sized nacre tablets in the mollusk shell.

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A Nacre Protein, n16.3, Self-Assembles To Form Protein Oligomers That Dimensionally Limit and Organize Mineral Deposits

et al. 2014

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“…Nature uses proteins to create three-dimensional mineralized structures that offer several important functions for biosurvival. [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18] However, there is uncertainty with regard to the role(s) that proteins play within different biomineral formation processes. For example, the nacre framework proteome 7,[10][11][12][13][14][15] are a collection of proteins affiliated with the beta-chitin polysaccharidesilk-like fibroin gel matrix that coats the exterior of aragonite tablets in the nacre layer of some mollusk shells.…”

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confidence: 99%

“…[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18] However, there is uncertainty with regard to the role(s) that proteins play within different biomineral formation processes. For example, the nacre framework proteome 7,[10][11][12][13][14][15] are a collection of proteins affiliated with the beta-chitin polysaccharidesilk-like fibroin gel matrix that coats the exterior of aragonite tablets in the nacre layer of some mollusk shells. 16 It is known that this macromolecular gel-like coating is an important medium for controlling calcium carbonate nucleation.…”

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confidence: 99%

Engineering of crystal surfaces and subsurfaces by framework biomineralization protein phases

et al. 2014

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“…38 n16 is a family of 108AA (amino acid chain length) ''aragonite promoter'' proteins, 39,40 named after their presence in nacre and their molecular weight in kDA. 23 polymorphic variants have been identified, all actively expressed in pearl oyster ( pinctada fucata), 41 while homologues of n16 have been found in other molluscs. [42][43][44] The 30AA N-terminal sequence of n16 shown in Fig.…”

Section: Biomineralisation and The N16n Peptidementioning

confidence: 99%

Testing the transferability of a coarse-grained model to intrinsically disordered proteins

Rutter

Brown

Quigley

et al. 2015

Phys. Chem. Chem. Phys.

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The intermediate-resolution coarse-grained protein model PLUM [T. Bereau and M. Deserno, J. Chem. Phys., 2009, 130, 235106] is used to simulate small systems of intrinsically disordered proteins involved in biomineralisation. With minor adjustments to reduce bias toward stable secondary structure, the model generates conformational ensembles conforming to structural predictions from atomistic simulation. Without additional structural information as input, the model distinguishes regions of the chain by predicted degree of disorder, manifestation of structure, and involvement in chain dimerisation. The model is also able to distinguish dimerisation behaviour between one intrinsically disordered peptide and a closely related mutant. We contrast this against the poor ability of PLUM to model the S1 quartz-binding peptide.

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Genetic structure and polymorphisms of the N16 gene in Pinctada fucata

Cited by 14 publications

References 21 publications

A Nacre Protein, n16.3, Self-Assembles To Form Protein Oligomers That Dimensionally Limit and Organize Mineral Deposits

A Nacre Protein, n16.3, Self-Assembles To Form Protein Oligomers That Dimensionally Limit and Organize Mineral Deposits

Engineering of crystal surfaces and subsurfaces by framework biomineralization protein phases

Testing the transferability of a coarse-grained model to intrinsically disordered proteins

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