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Aragonite-associated biomineralization proteins are disordered and contain interactive motifs.
MedLine Citation:
PMID:  23060620     Owner:  NLM     Status:  Publisher    
MOTIVATION: The formation of aragonite mineral in the mollusk shell or pearl nacre requires the participation of a diverse set of proteins that form the mineralized extracellular matrix. Although self-assembly processes have been identified for several nacre proteins, these proteins do not contain known globular protein-protein binding domains. Thus, we hypothesize that other sequence features are responsible for nacre matrix protein-protein assembly processes and ultimately aragonite biosynthesis. RESULTS: Out of 39 mollusk aragonite - associated protein sequences, 100% contain at least one region of intrinsic disorder or unfolding, with the highest percentages found in framework and pearl-associated proteins relative to the intracrystalline proteins. In some instances, these intrinsically disordered regions were identified as bind/fold sequences, and a limited number correlate with known biomineral-relevant sequences. Interestingly, 95% of the aragonite-associated protein sequences were found to contain at least one occurrence of amyloid-like or cross-beta strand aggregation-prone supersecondary motifs, and this correlates with known aggregation and aragonite formation functions in three experimentally tested protein sequences. Collectively, our findings indicate that aragonite-associated proteins have evolved signature sequence traits of intrinsic disorder and aggregation-prone regions that are important for their role(s) in matrix assembly and mineralization. CONTACT: SUPPLEMENTARY INFORMATION: Listing of aragonite-associated proteins (Table S1), listing of ANCHOR-positive sequences with known locations of Pro-X, Gly-X, and CDD-BLAST identified conserved domains (Table S2), CDD-BLAST conserved domain search results for CTLD, chitin-binding, and globular calcium-binding domains in ANCHOR - positive proteins (Table S3), histogram plots representing the percentage of intrinsic disorder for the aragonite-associated protein library (Figure S1) and location of aggregation-prone or amyloid-like motifs identified within known aragonite-stabilizing sequences (Figure S2) are available as supplementary data at Bioinformatics online.
John Spencer Evans
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-11
Journal Detail:
Title:  Bioinformatics (Oxford, England)     Volume:  -     ISSN:  1367-4811     ISO Abbreviation:  Bioinformatics     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9808944     Medline TA:  Bioinformatics     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Basic Sciences and Craniofacial Biology, Laboratory for Chemical Physics, New York University, 345 E. 24 Street, New York, NY 10012.
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