A Model Sea Urchin Spicule Matrix Protein, rSpSM50, Is a Hydrogelator That Modifies and Organizes the Mineralization Process

Gaurav Jain, Martin Pendola, Yu Chieh Huang, Denis Gebauer, John Spencer Evans

Research output: Contribution to journalArticle

Abstract

In the purple sea urchin Strongylocentrotus purpuratus, the formation and mineralization of fracture-resistant skeletal elements such as the embryonic spicule require the combinatorial participation of numerous spicule matrix proteins such as SpSM50. However, because of its limited abundance and solubility issues, it has been difficult to pursue extensive in vitro biochemical studies of SpSM50 protein and deduce its role in spicule formation and mineralization. To circumvent these problems, we expressed a tag-free bacterial model recombinant spicule matrix protein, rSpSM50. Bioinformatics and biophysical experiments confirm that rSpSM50 is an intrinsically disordered, aggregation-prone C-type lectin-like domain-containing protein that forms dimensionally and internally heterogeneous protein hydrogels that control the in vitro mineralization process in three ways. The hydrogels (1) kinetically stabilize the aqueous calcium carbonate system against nucleation and thermodynamically destabilize the initially formed ACC in bulk solution, (2) promote and organize faceted single-crystal calcite and polycrystalline vaterite nanoparticles, and (3) promote surface texturing of calcite crystals and induce subsurface nanoporosities and channels within both calcite and vaterite crystals. Many of these features are also common to mollusk shell nacre proteins and the sea urchin spicule matrix glycoprotein, SpSM30B/C, and we conclude that rSpSM50 is a spiculogenesis hydrogelator protein that exhibits traits found in other calcium carbonate mineral-modification proteins.

Original languageEnglish (US)
Pages (from-to)2663-2675
Number of pages13
JournalBiochemistry
Volume56
Issue number21
DOIs
StatePublished - May 30 2017

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Sea Urchins
Calcium Carbonate
Proteins
Enzyme Reactivators
Hydrogels
In Vitro Techniques
Anthralin
Carcinoid Tumor
Nacre
C-Type Lectins
Mollusca
Computational Biology
Tertiary Protein Structure
Nanoparticles
Solubility
Minerals
Glycoproteins
Edema Disease of Swine
Amino Acid Oxidoreductases
Common Bile Duct Diseases

ASJC Scopus subject areas

  • Biochemistry

Cite this

A Model Sea Urchin Spicule Matrix Protein, rSpSM50, Is a Hydrogelator That Modifies and Organizes the Mineralization Process. / Jain, Gaurav; Pendola, Martin; Huang, Yu Chieh; Gebauer, Denis; Evans, John Spencer.

In: Biochemistry, Vol. 56, No. 21, 30.05.2017, p. 2663-2675.

Research output: Contribution to journalArticle

Jain, Gaurav; Pendola, Martin; Huang, Yu Chieh; Gebauer, Denis; Evans, John Spencer / A Model Sea Urchin Spicule Matrix Protein, rSpSM50, Is a Hydrogelator That Modifies and Organizes the Mineralization Process.

In: Biochemistry, Vol. 56, No. 21, 30.05.2017, p. 2663-2675.

Research output: Contribution to journalArticle

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