A Model Sea Urchin Spicule Matrix Protein Self-Associates To Form Mineral-Modifying Protein Hydrogels

Gaurav Jain, Martin Pendola, Ashit Rao, Helmut Cölfen, John 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 the SpSM30A-F isoforms. However, because of limited abundance, it has been difficult to pursue extensive biochemical studies of the SpSM30 proteins and deduce their role in spicule formation and mineralization. To circumvent these problems, we expressed a model recombinant spicule matrix protein, rSpSM30B/C, which possesses the key sequence attributes of isoforms "B" and "C". Our findings indicate that rSpSM30B/C is expressed in insect cells as a single polypeptide containing variations in glycosylation that create microheterogeneity in rSpSM30B/C molecular masses. These post-translational modifications incorporate O- and N-glycans and anionic mono- and bisialylated and mono- and bisulfated monosaccharides on the protein molecules and enhance its aggregation propensity. Bioinformatics and biophysical experiments confirm that rSpSM30B/C is an intrinsically disordered, aggregation-prone protein that forms porous protein hydrogels that control the in vitro mineralization process in three ways: (1) increase the time interval for prenucleation cluster formation and transiently stabilize an ACC polymorph, (2) promote and organize single-crystal calcite nanoparticles, and (3) promote faceted growth and create surface texturing of calcite crystals. These features are also common to mollusk shell nacre proteins, and we conclude that rSpSM30B/C is a spiculogenesis protein that exhibits traits found in other calcium carbonate mineral modification proteins.

Original languageEnglish (US)
Pages (from-to)4410-4421
Number of pages12
JournalBiochemistry
Volume55
Issue number31
DOIs
StatePublished - Aug 9 2016

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Hydrogels
Sea Urchins
Minerals
Calcium Carbonate
Proteins
Strongylocentrotus purpuratus
Nacre
Protein Isoforms
Agglomeration
Carbonate minerals
Glycosylation
Monosaccharides
Texturing
Mollusca
Molecular mass
Post Translational Protein Processing
Bioinformatics
Protein C
Computational Biology
Polymorphism

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

Cite this

A Model Sea Urchin Spicule Matrix Protein Self-Associates To Form Mineral-Modifying Protein Hydrogels. / Jain, Gaurav; Pendola, Martin; Rao, Ashit; Cölfen, Helmut; Evans, John.

In: Biochemistry, Vol. 55, No. 31, 09.08.2016, p. 4410-4421.

Research output: Contribution to journalArticle

Jain, Gaurav ; Pendola, Martin ; Rao, Ashit ; Cölfen, Helmut ; Evans, John. / A Model Sea Urchin Spicule Matrix Protein Self-Associates To Form Mineral-Modifying Protein Hydrogels. In: Biochemistry. 2016 ; Vol. 55, No. 31. pp. 4410-4421.
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