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Biomineral proteins from Mytilus edulis mantle tissue transcriptome
Andy Freer1, Stephen Bridgett, Jiahong Jiang
1School of Chemistry, University of Glasgow, G12 8QQ, Glasgow, UK.
Marine Biotechnology (New York, N.Y.)
|July 6, 2013
Summary
Researchers profiled the transcriptome of the common blue mussel (Mytilus edulis) mantle tissue. This study identified novel shell biomineral proteins, enhancing our understanding of mussel shell formation.
Area of Science:
- Biomineralization research
- Marine biology
- Molecular biology
Background:
- The common blue mussel (Mytilus edulis) possesses a bimineralic shell composed of calcite and aragonite.
- Understanding the biological control of polymorph production is key to biomineralization research.
- Advances in sequencing technologies have increased the availability of transcriptome data for invertebrates.
Purpose of the Study:
- To profile the transcriptome of Mytilus edulis mantle tissue using pyrosequencing.
- To compare the effectiveness of different assembly programs for transcriptome analysis.
- To identify novel proteins involved in shell formation.
Main Methods:
- Roche 454 pyrosequencing was used to generate transcriptome data from Mytilus edulis mantle tissue.
- Multiple assembly programs (Roche Newbler, MIRA) were compared and their results merged using CAP3.
- Sequence similarity searches were performed against known shell protein databases.
Main Results:
- A comprehensive transcriptome for Mytilus edulis mantle tissue was generated.
- The study identified putative proteins with similarities to known shell proteins from other bivalves and gastropods.
- Crucially, transcripts encoding Shematrins and lysine-rich matrix proteins (KRMPs), previously undiscovered in Mytilus, were detected.
Conclusions:
- The enhanced transcriptome provides a valuable resource for studying Mytilus edulis shell biomineralization.
- The identification of novel proteins like Shematrins and KRMPs advances our knowledge of the molecular mechanisms underlying shell formation.
- This research contributes to understanding the diversity of shell matrix proteins across different marine invertebrates.
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