title: Silintaphin-1--interaction with silicatein during structure-guiding bio-silica formation.
abstract: Silicateins are unique enzymes of sponges (phylum Porifera) that template and catalyze the polymerization of nanoscale silicate to siliceous skeletal elements. These multifunctional spicules are often elaborately shaped, with complex symmetries. They carry an axial proteinaceous filament, consisting of silicatein and the scaffold protein silintaphin-1, which guides silica deposition and subsequent spicular morphogenesis. In vivo, the synthesis of the axial filament very likely proceeds in three steps: (a) assembly of silicatein monomers to form one pentamer; (b) assembly of pentamers to form fractal-like structures; and finally (c) assembly of fractal-like structures to form filaments. The present study was aimed at exploring the effect of self-assembled complexes of silicatein and silintaphin-1 on biosilica synthesis in vitro. Hence, in a comparative approach, recombinant silicatein and recombinant silintaphin-1 were used at different stoichiometric ratios to form axial filaments and to synthesize biosilica. Whereas recombinant silicatein-α reaggregates to randomly organized structures, coincubation of silicatein-α and silintaphin-1 (molecular ratio 4 : 1) resulted in synthetic filaments via fractal-like patterned self-assemblies, as observed by electron microscopy. Concurrently, owing to the concerted action of both proteins, the enzymatic activity of silicatein-α strongly increased by 5.3-fold (with the substrate tetraethyl orthosilicate), leading to significantly enhanced synthesis of biosilica. These results indicate that silicatein-α-mediated biosilicification depends on the concomitant presence of silicatein-α and silintaphin-1. Accordingly, silintaphin-1 might not only enhance the enzymatic activity of silicatein-α, but also accelerate the nonenzymatic polycondensation of the silica product before releasing the fully synthesized biosiliceous polymer.
authors.affiliation: Institute for Physiological Chemistry, Johannes Gutenberg-University, Medical School, Mainz, Germany.
authors.forename: Ute
authors.initials: U
authors.lastname: Schlossmacher
authors.forename: Matthias
authors.initials: M
authors.lastname: Wiens
authors.forename: Heinz C
authors.initials: HC
authors.lastname: Schröder
authors.forename: Xiaohong
authors.initials: X
authors.lastname: Wang
authors.forename: Klaus P
authors.initials: KP
authors.lastname: Jochum
authors.forename: Werner E G
authors.initials: WE
authors.lastname: Müller
mesh_terms: D000818:Animals; D002403:Cathepsins / Q000235:genetics / Q000378:metabolism*; D054118:Nanospheres / Q000737:chemistry / Q000648:ultrastructure; D011161:Porifera / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012822:Silicon Dioxide / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; C112571:silicatein alpha; D012822:Silicon Dioxide; D002403:Cathepsins