Structure-function studies of the lustrin A polyelectrolyte domains, RKSY and D4

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

Research output: Contribution to journalArticle

Abstract

The lustrin superfamily represents a unique group of biomineralization proteins localized between layered aragonite mineral plates (i.e., nacre layers) in mollusk shell. These proteins not only exhibit elastomeric behavior within the mineralized matrix, but also adhesion to the aragonite-containing composite layer. One member of the lustrin superfamily, Lustrin A, has been sequenced; the protein is organized into defined, modular sequence domains that are hypothesized to perform separate functions (i.e., force unfolding, mineral adhesion, intermolecular binding) within the Lustrin A protein. Using nuclear magnetic resonance (NMR) and in vitro mineralization assays, we investigated structure-function relationships for two Lustrin A putative mineral binding domains, the 30 AA Arg, Lys, Tyr, Ser-rich (RKSY) and the 24 AA Asp-rich (D4) sequence regions domain of the Lustrin A protein. The results indicate that both sequences adopt open, unfolded structures that represent either extended or random coil states. Using geologic calcite overgrowth assays and scanning electron microscopic analyses, we observe that the RKSY polypeptide does not significantly perturb calcium carbonate growth. However, the D4 domain does influence crystal growth in a concentration-dependent manner. Collectively, our data indicate that D4, and not the RKSY domain, exhibits structure-function activity consistent with a mineral binding region.

Original languageEnglish (US)
Pages (from-to)10-15
Number of pages6
JournalConnective Tissue Research
Volume44
Issue numberSUPPL. 1
StatePublished - 2003

Fingerprint

Polyelectrolytes
Calcium Carbonate
Minerals
Proteins
Assays
Nacre
Adhesion
Biomineralization
Mollusca
Crystallization
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
lustrin A
Electrons
Scanning
Peptides
Composite materials
Growth

Keywords

  • Biomineralization
  • Lustrin A
  • Polyelectrolyte
  • Secondary structure

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Nephrology
  • Cell Biology
  • Orthopedics and Sports Medicine

Cite this

Structure-function studies of the lustrin A polyelectrolyte domains, RKSY and D4. / Wustman, Brandon A.; Weaver, James C.; Morse, Daniel E.; Evans, John.

In: Connective Tissue Research, Vol. 44, No. SUPPL. 1, 2003, p. 10-15.

Research output: Contribution to journalArticle

Wustman, BA, Weaver, JC, Morse, DE & Evans, J 2003, 'Structure-function studies of the lustrin A polyelectrolyte domains, RKSY and D4', Connective Tissue Research, vol. 44, no. SUPPL. 1, pp. 10-15.
Wustman, Brandon A. ; Weaver, James C. ; Morse, Daniel E. ; Evans, John. / Structure-function studies of the lustrin A polyelectrolyte domains, RKSY and D4. In: Connective Tissue Research. 2003 ; Vol. 44, No. SUPPL. 1. pp. 10-15.
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