Characterization of a Ca(II)-, Mineral-Interactive Polyelectrolyte Sequence from the Adhesive Elastomeric Biomineralization Protein Lustrin A

Wustman, Brandon A.; Weaver, James C.; Morse, Daniel E.; Evans, John Spencer

doi:10.1021/la034857w

Cited by 32 publications

(143 citation statements)

References 45 publications

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“…In parallel with the sequencing studies, model peptide studies were conducted to identify and characterize mineral binding domains from both proteins. We show here that the 1–30‐residue N‐terminal domains of both mature protein sequences exhibit binding to growth step regions of growing calcite, and possess random coil, extended secondary structures consistent with other demonstrated calcite binding domains 11…”

Section: Introductionsupporting

confidence: 83%

“…The 1–30 AA N‐terminal domains of the prepro‐processed, mature AP7 and AP24 primary sequences possess Ca(II) binding residues (Asp, Glu) as well as putative carbonate interaction residues (Thr, Ser, Arg, Lys, Tyr),11, 15, 16 and thus were singled out as initial candidates for calcite interaction studies. Two C‐amide “capped” 30‐mer polypeptides were synthesized, corresponding to the 1–30 residue N‐terminal regions of AP7 (designated as AP7‐1) and AP24 (AP24‐1).…”

Section: Methodsmentioning

confidence: 99%

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Characterization of two molluscan crystal‐modulating biomineralization proteins and identification of putative mineral binding domains

et al. 2003

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Ethylenediamine-tetraacetic acid extracted water-soluble matrix proteins in molluscan shells secreted from the mantle epithelia are believed to control crystal nucleation, morphology, orientation, and phase of the deposited mineral. Previously, atomic force microscopy demonstrated that abalone nacre proteins bind to growing step edges and to specific crystallographic faces of calcite, suggesting that inhibition of calcite growth may be one of the molecular processes required for growth of the less thermodynamically stable aragonite phase. Previous experiments were done with protein mixtures. To elucidate the role of single proteins, we have characterized two proteins isolated from the aragonitic component of nacre of the red abalone, Haliotis rufescens. These proteins, purified by hydrophobic interaction chromatography, are designated AP7 and AP24 (aragonitic protein of molecular weight 7 kDa and 24 kDa, respectively). Degenerate oligonucleotide primers corresponding to N-terminal and internal peptide sequences were used to amplify cDNA clones by a polymerase chain reaction from a mantle cDNA library; the deduced primary amino acid sequences are presented. Preliminary crystal growth experiments demonstrate that protein fractions enriched in AP7 and AP24 produced CaCO(3) crystals with morphology distinct from crystals grown in the presence of the total mixture of soluble aragonite-specific proteins. Peptides corresponding to the first 30 residues of the N-terminal sequences of both AP7 and AP24 were generated. The synthetic peptides frustrate the progression of step edges of a growing calcite surface, indicating that sequence features within the N-termini of AP7 and AP24 include domains that interact with CaCO(3). CD analyses demonstrate that the N-terminal peptide sequences do not possess significant percentages of alpha-helix or beta-strand secondary structure in solution. Instead, in both the presence and absence of Ca(II), the peptides retain unfolded conformations that may facilitate protein-mineral interaction.

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Section: Introductionsupporting

confidence: 83%

Section: Methodsmentioning

confidence: 99%

Characterization of two molluscan crystal‐modulating biomineralization proteins and identification of putative mineral binding domains

et al. 2003

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“…Some of these (9 of 22) are expressed homogenously in one or more zones responsible for the creation of different shell layers. For example, LustrinA , first isolated from Haliotis rufescens , the gene product of which contributes to the elastomeric properties of the nacreous layer [11,27,47-50], is expressed, along with two other novel genes, in the mantle territory responsible for the production of the inner nacreous layer (Figure 3X–Z). Other evolutionarily conserved genes, including calmodulin and a calcium-binding protein, are expressed continuously along the length of the mantle within both the inner fold and the anterior crease of the outer fold (Figure 3I–L), while others, such as ferritin, are expressed only in the outer fold (Figure 3M, N).…”

Section: Resultsmentioning

confidence: 99%

A rapidly evolving secretome builds and patterns a sea shell

et al. 2006

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Background: Instructions to fabricate mineralized structures with distinct nanoscale architectures, such as seashells and coral and vertebrate skeletons, are encoded in the genomes of a wide variety of animals. In mollusks, the mantle is responsible for the extracellular production of the shell, directing the ordered biomineralization of CaCO 3 and the deposition of architectural and color patterns. The evolutionary origins of the ability to synthesize calcified structures across various metazoan taxa remain obscure, with only a small number of protein families identified from molluskan shells. The recent sequencing of a wide range of metazoan genomes coupled with the analysis of gene expression in non-model animals has allowed us to investigate the evolution and process of biomineralization in gastropod mollusks.

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“…Extracted from the nacreous layer of the abalone H. rufescens, this modular structure has been the subject of several studies to try and elucidate structure-function relationships. [237][238][239][240][241] Perlustrin, 242,243 perlucin, 242,244 perlwapin, 245 and perlinhibin 246 are four proteins isolated from the nacreous layer of the abalone H. laeVigata.…”

Section: Bivalve Molluscssorganic Compositionmentioning

confidence: 99%