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First published online June 26, 2009
Journal of Experimental Biology 212, 2224-2236 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.029686

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Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis

Jason Sagert and J. Herbert Waite^*

Marine Science Institute, University of California, Santa Barbara, CA 93106, USA

^* Author for correspondence (e-mail: waite{at}lifesci.ucsb.edu)

Accepted 8 April 2009

The marine mussel Mytilus galloprovincialis is tethered to rocks in the intertidal zone by a holdfast known as the byssus. Functioning as a shock absorber, the byssus is composed of threads, the primary molecular components of which are collagen-containing proteins (preCOLs) that largely dictate the higher order self-assembly and mechanical properties of byssal threads. The threads contain additional matrix components that separate and perhaps lubricate the collagenous microfibrils during deformation in tension. In this study, the thread matrix proteins (TMPs), a glycine-, tyrosine- and asparagine-rich protein family, were shown to possess unique repeated sequence motifs, significant transcriptional heterogeneity and were distributed throughout the byssal thread. Deamidation was shown to occur at a significant rate in a recombinant TMP and in the byssal thread as a function of time. Furthermore, charge heterogeneity presumably due to deamidation was observed in TMPs extracted from threads. The TMPs were localized to the preCOL-containing secretory granules in the collagen gland of the foot and are assumed to provide a viscoelastic matrix around the collagenous fibers in byssal threads.

Key words: byssal threads, hyperinstability, asparagine-rich, deamidation, thread matrix protein, marine mussel, Mytilus galloprovincialis, decomposition

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