A basic protein, N25, from a mollusk modifies calcium carbonate morphology and shell biomineralization.

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  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Animal Shells*/chemistry ; Animal Shells*/metabolism ; Calcium Carbonate*/chemistry ; Calcium Carbonate*/metabolism ; Extracellular Matrix Proteins*/chemistry ; Extracellular Matrix Proteins*/genetics ; Extracellular Matrix Proteins*/metabolism; Animals ; HEK293 Cells ; Humans ; Pinctada/genetics ; Pinctada/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
    • Abstract:
      Biomineralization is a widespread biological process in the formation of shells, teeth, or bones. Matrix proteins in biominerals have been widely investigated for their roles in directing biomineralization processes such as crystal morphologies, polymorphs, and orientations. Here, we characterized a basic matrix protein, named mantle protein N25 (N25), identified previously in the Akoya pearl oyster ( Pinctada fucata ). Unlike some known acidic matrix proteins containing Asp or Glu as possible Ca 2+ -binding residues, we found that N25 is rich in Pro (12.4%), Ser (12.8%), and Lys (8.8%), suggesting it may perform a different function. We used the recombinant protein purified by refolding from inclusion bodies in a Ca(HCO 3 ) 2 supersaturation system and found that it specifically affects calcite morphologies. An X-ray powder diffraction (XRD) assay revealed that N25 could help delay the transformation of vaterites (a metastable calcium carbonate polymorph) to calcite. We also used fluorescence super-resolution imaging to map the distribution of N25 in CaCO 3 crystals and transfected a recombinant N25-EGFP vector into HEK-293T cells to mimic the native process in which N25 is secreted by mantle epithelial cells and integrated into mineral structures. Our observations suggest N25 specifically affects crystal morphologies and provide evidence that basic proteins lacking acidic groups can also direct biomineralization. We propose that the attachment of N25 to specific sites on CaCO 3 crystals may inhibit some crystal polymorphs or morphological transformation.
      (© 2019 Yang et al.)
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    • Contributed Indexing:
      Keywords: N25; attachment energy; biomineralization; calcite binding protein; extracellular matrix protein; morphological simulation; protein folding; protein secretion; vesicles
    • Accession Number:
      0 (Extracellular Matrix Proteins)
      0 (Recombinant Proteins)
      H0G9379FGK (Calcium Carbonate)
    • Publication Date:
      Date Created: 20190411 Date Completed: 20191209 Latest Revision: 20210314
    • Publication Date:
      20231215
    • Accession Number:
      PMC6544838
    • Accession Number:
      10.1074/jbc.RA118.007338
    • Accession Number:
      30967473