Biomineralization proteins: from vertebrates to bacteria
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Biomineralization processes are frequently found in nature. Living organisms use various strategies to create highly ordered and hierarchical mineral structures under physiologic conditions in which the temperatures and pressures are much lower than those required to form the same mineralized structures by chemical synthesis. Although the mechanism of biomineralization remains elusive, proteins have been found responsible for the formation of such mineral structures in many cases. These proteins are active components in the process of biomineralization. The mechanisms by which their function can vary from providing active organic matrices that control the formation of specific mineral structures to being catalysts that facilitate the crystallization of certain metal ions. This review summarizes the current understanding of the functions of several representative biomineralization proteins from vertebrates to bacteria in the hopes of providing useful insight and guidance for further elucidation of mechanisms of biomineralization processes in living organisms.
Keywordsbiomineralization proteins structure-function relationships self-assembly nanoparticles
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- Brinker C J, Scherrer G W (1990). Sol-gel science: the chemistry of solgel processing. New York: Academic PressGoogle Scholar
- Du C, Falini G, Fermani S, Abbott C, Moradian-Oldak J (2005a). Corrections and clarifications. Science, 309(5744): 2166Google Scholar
- Hodge A, Petruska J (1963). Aspects of Protein Structure. New York: Academic PressGoogle Scholar
- Mahamid J, Aichmayer B, Shimoni E, Ziblat R, Li C, Siegel S, Paris O, Fratzl P, Weiner S, Addadi L (2010). Mapping amorphous calcium phosphate transformation into crystalline mineral from the cell to the bone in zebrafish fin rays. Proc Natl Acad Sci USA, 107(14): 6316–6321PubMedCrossRefGoogle Scholar
- Müller W E G, Boreiko A, Schlossmacher U, Wang X, Tahir M N, Tremel W, Brandt D, Kaandorp J A, Schröder H C (2007). Fractalrelated assembly of the axial filament in the demosponge Suberites domuncula: relevance to biomineralization and the formation of biogenic silica. Biomaterials, 28(30): 4501–4511PubMedCrossRefGoogle Scholar
- Pozzolini M, Sturla L, Cerrano C, Bavestrello G, Camardella L, Parodi A M, Raheli F, Benatti U, Müller WEG, Giovine M (2004). Molecular cloning of silicatein gene from marine sponge Petrosia ficiformis (Porifera, Demospongiae) and development of primmorphs as a model for biosilicification studies. Mar Biotechnol (NY), 6(6): 594–603CrossRefGoogle Scholar
- Richter M, Kube M, Bazylinski D A, Lombardot T, Glöckner F O, Reinhardt R, Schüler D (2007). Comparative genome analysis of four magnetotactic bacteria reveals a complex set of group-specific genes implicated in magnetosome biomineralization and function. J Bacteriol, 189(13): 4899–4910PubMedCrossRefGoogle Scholar
- Schröder H C, PeroviĆ-Ottstadt S, Rothenberger M, Wiens M, Schwertner H, Batel R, Korzhev M, Müller I M, Müller W E G (2004a). Silica transport in the demosponge Suberites domuncula: fluorescence emission analysis using the PDMPO probe and cloning of a potential transporter. Biochem J, 381(Pt 3): 665–673PubMedGoogle Scholar
- Uebe R, Junge K, Henn V, Poxleitner G, Katzmann E, Plitzko J M, Zarivach R, Kasama T, Wanner G, Pósfai M, Böttger L, Matzanke B, Schüler D (2011). The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol Microbiol, 82(4): 818–835PubMedCrossRefGoogle Scholar
- Wang L, Prozorov T, Palo P E, Liu X, Vaknin D, Prozorov R, Mallapragada S, Nilsen-Hamilton M (2012a). Self-assembly and biphasic iron-binding characteristics of Mms6, a bacterial protein that promotes the formation of superparamagnetic magnetite nanoparticles of uniform size and shape. Biomacromolecules, 13(1): 98–105PubMedCrossRefGoogle Scholar
- Wang W, Bu W, Wang L, Palo P E, Mallapragada S, Nilsen-Hamilton M, Vaknin D (2012b). Interfacial properties and iron binding to bacterial proteins that promote the growth of magnetite nanocrystals: X-ray reflectivity and surface spectroscopy studies. Langmuir, 28(9): 4274–4282PubMedCrossRefGoogle Scholar