Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 10, Pages 3788-3793Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1301419110
Keywords
acid-rich proteins; collagen; cadherin; carbonic anhdyrase
Categories
Funding
- National Science Foundation [EF1041143]
- Emerging Frontiers
- Direct For Biological Sciences [1041143] Funding Source: National Science Foundation
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It has long been recognized that a suite of proteins exists in coral skeletons that is critical for the oriented precipitation of calcium carbonate crystals, yet these proteins remain poorly characterized. Using liquid chromatography-tandem mass spectrometry analysis of proteins extracted from the cell-free skeleton of the hermatypic coral, Stylophora pistillata, combined with a draft genome assembly from the cnidarian host cells of the same species, we identified 36 coral skeletal organic matrix proteins. The proteome of the coral skeleton contains an assemblage of adhesion and structural proteins as well as two highly acidic proteins that may constitute a unique coral skeletal organic matrix protein subfamily. We compared the 36 skeletal organic matrix protein sequences to genome and transcriptome data from three other corals, three additional invertebrates, one vertebrate, and three single-celled organisms. This work represents a unique extensive proteomic analysis of biomineralization-related proteins in corals from which we identify a biomineralization toolkit, an organic scaffold upon which aragonite crystals can be deposited in specific orientations to form a phenotypically identifiable structure.
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