Intrinsically Disordered and Pliable Starmaker-Like Protein from Medaka (Oryzias latipes) Controls the Formation of Calcium Carbonate Crystals

Please always quote using this URN: urn:nbn:de:bvb:20-opus-114251
  • 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 inFish 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.show moreshow less

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Metadaten
Author: Miroslawa Rozycka, Magdalena Wojtas, Michal Jakob, Christian Stigloher, Mikolaj Grzeszkowiak, Maciej Mazur, Andrzej Ozyhar
URN:urn:nbn:de:bvb:20-opus-114251
Document Type:Journal article
Faculties:Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften
Language:English
Parent Title (English):PLOS ONE
ISSN:1932-6203
Year of Completion:2014
Volume:9
Issue:12
Source:PLoS ONE 9(12): e114308. doi:10.1371/journal.pone.0114308
DOI:https://doi.org/10.1371/journal.pone.0114308
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=25490041
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
Tag:alpha-helical structure; biominarlization proteins; circular-dichroism; dye stains-all; modulating; nacreous layer formation; olyelectrolyte domains; phosphorylation sites; polyelectrolyte domains; procambarus-clarkii; secondary structure; unstructured proteins
Release Date:2015/06/26
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung