|Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis.
|Year of Publication
|Sagert, J, Waite, JH
|J Exp Biol
|Amino Acid Sequence, Animals, Base Sequence, Collagen, DNA, Complementary, Extracellular Matrix Proteins, Molecular Sequence Data, Multigene Family, Mytilus, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid
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.
|J. Exp. Biol.
|PubMed Central ID
|R01 DE 015415 / DE / NIDCR NIH HHS / United States
R01 DE 018468 / DE / NIDCR NIH HHS / United States
R01 DE015415 / DE / NIDCR NIH HHS / United States
R01 DE015415-04 / DE / NIDCR NIH HHS / United States
R01 DE018468 / DE / NIDCR NIH HHS / United States
R01 DE018468-01A1 / DE / NIDCR NIH HHS / United States