Co-expression and functional interaction of silicatein with galectin: matrix-guided formation of siliceous spicules in the marine demosponge Suberites domuncula.
Sponges (phylum Porifera) of the class of Demospongiae are stabilized by a siliceous skeleton. It is composed of silica needles (spicules), which provide the morphogenetic scaffold of these metazoans. In the center of the spicules there is an axial filament that consists predominantly of silicatein, an enzyme that catalyzes the synthesis of biosilica. By differential display of transcripts we identified additional proteins involved in silica formation. Two genes were isolated from the marine demosponge Suberites domuncula; one codes for a galectin and the other for a fibrillar collagen. The galectin forms aggregates to which silicatein molecules bind. The extent of the silicatein-mediated silica formation strongly increased if associated with the galectin. By applying a new and mild extraction procedure that avoids hydrogen fluoride treatment, native axial filaments were extracted from spicules of S. domuncula. These filaments contained, in addition to silicatein, the galectin and a few other proteins. Immunogold electron microscopic studies underscored the role of these additional proteins, in particular that of galectin, in spiculogenesis. Galectin, in addition to silicatein, presumably forms in the axial canal as well as on the surface of the spicules an organized net-like matrix. In the extraspicular space most of these complexes are arranged concentrically around the spicules. Taken together, these additional proteins, working together with silicatein, may also be relevant for potential (nano)-biotechnological applications of silicatein in the formation of surface coatings. Finally, we propose a scheme that outlines the matrix (galectin/silicatein)-guided appositional growth of spicules through centripetal and centrifugal synthesis and deposition of biosilica.
Schröder
Heinz C
HC
Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität Mainz, Duesbergweg 6, D-55099 Mainz, Germany.
Boreiko
Alexandra
A
Korzhev
Michael
M
Tahir
Muhammad N
MN
Tremel
Wolfgang
W
Eckert
Carsten
C
Ushijima
Hiroshi
H
Müller
Isabel M
IM
Müller
Werner E G
WE
D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000378:metabolism*; D005260:Female; D024022:Fibrillar Collagens / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D037501:Galectin 2 / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D020869:Gene Expression Profiling; D007150:Immunohistochemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology; D011817:Rabbits; D011994:Recombinant Proteins; D017386:Sequence Homology, Amino Acid; D012822:Silicon Dioxide / Q000378:metabolism*; D047233:Suberites / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*
D024022:Fibrillar Collagens; D037501:Galectin 2; D010446:Peptide Fragments; D011994:Recombinant Proteins; C112571:silicatein alpha; D012822:Silicon Dioxide; D002403:Cathepsins