title: Intrinsically disordered and pliable Starmaker-like protein from medaka (Oryzias latipes) controls the formation of calcium carbonate crystals.
abstract: Fish otoliths, biominerals composed of calcium carbonate with a small amount of organic matrix, are involved in the functioning of the inner ear. Starmaker (Stm) from zebrafish (Danio rerio) was the first protein found to be capable of controlling the formation of otoliths. Recently, a gene was identified encoding the Starmaker-like (Stm-l) protein from medaka (Oryzias latipes), a putative homologue of Stm and human dentine sialophosphoprotein. Although there is no sequence similarity between Stm-l and Stm, Stm-l was suggested to be involved in the biomineralization of otoliths, as had been observed for Stm even before. The molecular properties and functioning of Stm-l as a putative regulatory protein in otolith formation have not been characterized yet. A comprehensive biochemical and biophysical analysis of recombinant Stm-l, along with in silico examinations, indicated that Stm-l exhibits properties of a coil-like intrinsically disordered protein. Stm-l possesses an elongated and pliable structure that is able to adopt a more ordered and rigid conformation under the influence of different factors. An in vitro assay of the biomineralization activity of Stm-l indicated that Stm-l affected the size, shape and number of calcium carbonate crystals. The functional significance of intrinsically disordered properties of Stm-l and the possible role of this protein in controlling the formation of calcium carbonate crystals is discussed.
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
authors.forename: Mirosława
authors.initials: M
authors.lastname: Różycka
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
authors.forename: Magdalena
authors.initials: M
authors.lastname: Wojtas
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
authors.forename: Michał
authors.initials: M
authors.lastname: Jakób
authors.affiliation: Division of Electron Microscopy, Biocenter, University of Würzburg, Würzburg, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Stigloher
authors.affiliation: NanoBioMedical Centre and Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University, Poznań, Poland.
authors.forename: Mikołaj
authors.initials: M
authors.lastname: Grzeszkowiak
authors.affiliation: Department of Chemistry, University of Warsaw, Warsaw, Poland.
authors.forename: Maciej
authors.initials: M
authors.lastname: Mazur
authors.affiliation: Department of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
authors.forename: Andrzej
authors.initials: A
authors.lastname: Ożyhar
mesh_terms: D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D029941:Fish Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D057446:Hydrodynamics; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008903:Minerals / Q000378:metabolism; D009990:Oryzias; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D029961:Zebrafish Proteins / Q000737:chemistry*
chemical_list: D029941:Fish Proteins; D064267:Intrinsically Disordered Proteins; D008903:Minerals; D029961:Zebrafish Proteins; C478248:stm protein, zebrafish; D002119:Calcium Carbonate