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Elsevier, Journal of Biological Chemistry, 23(287), p. 19367-19376, 2012

DOI: 10.1074/jbc.m112.352005

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Molecular Cloning and Characterization of First Organic Matrix Protein from Sclerites of Red Coral, Corallium rubrum*

Journal article published in 2012 by Julien Debreuil, Eric Tambutté, Éric Tambutté, Didier Zoccola ORCID, Emeline Deleury, Jean-Marie Guigonis, Michel Samson, Denis Allemand, Sylvie Tambutté
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

We report here for the first time the isolation and characterization of a protein from the organic matrix (OM) of the sclerites of the alcyonarian, Corallium rubrum. This protein named scleritin is one of the predominant proteins extracted from the EDTA-soluble fraction of the OM. The entire open reading frame (ORF) was obtained by comparing amino acid sequences from de novo mass spectrometry and Edman degradation with an expressed sequence tag library dataset of C. rubrum. Scleritin is a secreted basic phosphorylated protein which exhibits a short amino acid sequence of 135 amino acids and a signal peptide of 20 amino acids. From specific antibodies raised against peptide sequences of scleritin, we obtained immunolabeling of scleroblasts and OM of the sclerites which provides information on the biomineralization pathway in C. rubrum.