Starmaker Exhibits Properties of an Intrinsically Disordered Protein
Fish otoliths composed of calcium carbonate and an organic matrix play a primary role in gravity sensing and the perception of sound. Starmaker (Stm) was the first protein found to be capable of influencing the process of biomineralization of otoliths. Stm dictates the shape, size, and selection of...
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Veröffentlicht in: | Biomacromolecules 2008-08, Vol.9 (8), p.2118-2125 |
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creator | Kapłon, Tomasz M Rymarczyk, Grzegorz Nocula-Ługowska, Małgorzata Jakób, Michał Kochman, Marian Lisowski, Marek Szewczuk, Zbigniew Ożyhar, Andrzej |
description | Fish otoliths composed of calcium carbonate and an organic matrix play a primary role in gravity sensing and the perception of sound. Starmaker (Stm) was the first protein found to be capable of influencing the process of biomineralization of otoliths. Stm dictates the shape, size, and selection of calcium carbonate polymorphs in a concentration-dependent manner. To facilitate exploration of the molecular basis of Stm function, we have developed and optimized a protocol for efficient expression and purification of the homogeneous nontagged Stm. The homogeneous nontagged Stm corresponds to its functional form, which is devoid of a signal peptide. A comprehensive biochemical and biophysical analysis of recombinant Stm, along with in silico examinations, indicate for the first time that Stm exhibits the properties of intrinsically disordered proteins. The functional significance of Stm having intrinsically disordered protein properties and its possible role in controlling the formation of otoliths is discussed. |
doi_str_mv | 10.1021/bm800135m |
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Starmaker (Stm) was the first protein found to be capable of influencing the process of biomineralization of otoliths. Stm dictates the shape, size, and selection of calcium carbonate polymorphs in a concentration-dependent manner. To facilitate exploration of the molecular basis of Stm function, we have developed and optimized a protocol for efficient expression and purification of the homogeneous nontagged Stm. The homogeneous nontagged Stm corresponds to its functional form, which is devoid of a signal peptide. A comprehensive biochemical and biophysical analysis of recombinant Stm, along with in silico examinations, indicate for the first time that Stm exhibits the properties of intrinsically disordered proteins. The functional significance of Stm having intrinsically disordered protein properties and its possible role in controlling the formation of otoliths is discussed.</description><identifier>ISSN: 1525-7797</identifier><identifier>EISSN: 1526-4602</identifier><identifier>DOI: 10.1021/bm800135m</identifier><identifier>PMID: 18636772</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Biological and medical sciences ; Biophysics - methods ; Calcium Carbonate - chemistry ; Dose-Response Relationship, Drug ; Fishes ; Fundamental and applied biological sciences. Psychology ; Genetic Vectors ; Molecular biophysics ; Otolithic Membrane - physiology ; Protein Conformation ; Protein Sorting Signals ; Protein Structure, Tertiary ; Recombinant Proteins - chemistry ; Spectrometry, Mass, Electrospray Ionization - methods ; Spectrophotometry, Ultraviolet - methods ; Structure in molecular biology ; Tridimensional structure ; Zebrafish ; Zebrafish Proteins - chemistry</subject><ispartof>Biomacromolecules, 2008-08, Vol.9 (8), p.2118-2125</ispartof><rights>Copyright © 2008 American Chemical Society</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a375t-e35372bc8f8869d9b95ba8d332345eca4fde23b1b7849d8c0ef89682175101153</citedby><cites>FETCH-LOGICAL-a375t-e35372bc8f8869d9b95ba8d332345eca4fde23b1b7849d8c0ef89682175101153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bm800135m$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bm800135m$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20613096$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18636772$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kapłon, Tomasz M</creatorcontrib><creatorcontrib>Rymarczyk, Grzegorz</creatorcontrib><creatorcontrib>Nocula-Ługowska, Małgorzata</creatorcontrib><creatorcontrib>Jakób, Michał</creatorcontrib><creatorcontrib>Kochman, Marian</creatorcontrib><creatorcontrib>Lisowski, Marek</creatorcontrib><creatorcontrib>Szewczuk, Zbigniew</creatorcontrib><creatorcontrib>Ożyhar, Andrzej</creatorcontrib><title>Starmaker Exhibits Properties of an Intrinsically Disordered Protein</title><title>Biomacromolecules</title><addtitle>Biomacromolecules</addtitle><description>Fish otoliths composed of calcium carbonate and an organic matrix play a primary role in gravity sensing and the perception of sound. Starmaker (Stm) was the first protein found to be capable of influencing the process of biomineralization of otoliths. Stm dictates the shape, size, and selection of calcium carbonate polymorphs in a concentration-dependent manner. To facilitate exploration of the molecular basis of Stm function, we have developed and optimized a protocol for efficient expression and purification of the homogeneous nontagged Stm. The homogeneous nontagged Stm corresponds to its functional form, which is devoid of a signal peptide. A comprehensive biochemical and biophysical analysis of recombinant Stm, along with in silico examinations, indicate for the first time that Stm exhibits the properties of intrinsically disordered proteins. The functional significance of Stm having intrinsically disordered protein properties and its possible role in controlling the formation of otoliths is discussed.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biophysics - methods</subject><subject>Calcium Carbonate - chemistry</subject><subject>Dose-Response Relationship, Drug</subject><subject>Fishes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Vectors</subject><subject>Molecular biophysics</subject><subject>Otolithic Membrane - physiology</subject><subject>Protein Conformation</subject><subject>Protein Sorting Signals</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Spectrometry, Mass, Electrospray Ionization - methods</subject><subject>Spectrophotometry, Ultraviolet - methods</subject><subject>Structure in molecular biology</subject><subject>Tridimensional structure</subject><subject>Zebrafish</subject><subject>Zebrafish Proteins - chemistry</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90MtKAzEUgOEgiq3VhS8gs1FxMZr7ZSlt1UJBQV0PSSaDqXOpyQzYt3dqS7sRVzmLj3PCD8A5grcIYnRnKgkhIqw6AEPEME8ph_jwd2apEEoMwEmMCwihIpQdgwGSnHAh8BBMXlsdKv3pQjL9_vDGtzF5Cc3Shda7mDRFoutkVrfB19FbXZarZOJjE3IXXL6WrfP1KTgqdBnd2fYdgfeH6dv4KZ0_P87G9_NUE8Ha1BFGBDZWFlJylSujmNEyJwT3v3JW0yJ3mBhkhKQqlxa6QiouMRIMQYQYGYHrzd5laL46F9us8tG6stS1a7qYCUYZVYjSXl79K7miUECCenizgTY0MQZXZMvgKx1WGYLZOm62i9vbi-3SzlQu38ttzR5cboGOfasi6Nr6uHMYckSg4nunbcwWTRfqvtofB38A9UmMKw</recordid><startdate>20080801</startdate><enddate>20080801</enddate><creator>Kapłon, Tomasz M</creator><creator>Rymarczyk, Grzegorz</creator><creator>Nocula-Ługowska, Małgorzata</creator><creator>Jakób, Michał</creator><creator>Kochman, Marian</creator><creator>Lisowski, Marek</creator><creator>Szewczuk, Zbigniew</creator><creator>Ożyhar, Andrzej</creator><general>American Chemical Society</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QO</scope><scope>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20080801</creationdate><title>Starmaker Exhibits Properties of an Intrinsically Disordered Protein</title><author>Kapłon, Tomasz M ; Rymarczyk, Grzegorz ; Nocula-Ługowska, Małgorzata ; Jakób, Michał ; Kochman, Marian ; Lisowski, Marek ; Szewczuk, Zbigniew ; Ożyhar, Andrzej</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a375t-e35372bc8f8869d9b95ba8d332345eca4fde23b1b7849d8c0ef89682175101153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biophysics - methods</topic><topic>Calcium Carbonate - chemistry</topic><topic>Dose-Response Relationship, Drug</topic><topic>Fishes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Vectors</topic><topic>Molecular biophysics</topic><topic>Otolithic Membrane - physiology</topic><topic>Protein Conformation</topic><topic>Protein Sorting Signals</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Spectrometry, Mass, Electrospray Ionization - methods</topic><topic>Spectrophotometry, Ultraviolet - methods</topic><topic>Structure in molecular biology</topic><topic>Tridimensional structure</topic><topic>Zebrafish</topic><topic>Zebrafish Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kapłon, Tomasz M</creatorcontrib><creatorcontrib>Rymarczyk, Grzegorz</creatorcontrib><creatorcontrib>Nocula-Ługowska, Małgorzata</creatorcontrib><creatorcontrib>Jakób, Michał</creatorcontrib><creatorcontrib>Kochman, Marian</creatorcontrib><creatorcontrib>Lisowski, Marek</creatorcontrib><creatorcontrib>Szewczuk, Zbigniew</creatorcontrib><creatorcontrib>Ożyhar, Andrzej</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biomacromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kapłon, Tomasz M</au><au>Rymarczyk, Grzegorz</au><au>Nocula-Ługowska, Małgorzata</au><au>Jakób, Michał</au><au>Kochman, Marian</au><au>Lisowski, Marek</au><au>Szewczuk, Zbigniew</au><au>Ożyhar, Andrzej</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Starmaker Exhibits Properties of an Intrinsically Disordered Protein</atitle><jtitle>Biomacromolecules</jtitle><addtitle>Biomacromolecules</addtitle><date>2008-08-01</date><risdate>2008</risdate><volume>9</volume><issue>8</issue><spage>2118</spage><epage>2125</epage><pages>2118-2125</pages><issn>1525-7797</issn><eissn>1526-4602</eissn><abstract>Fish otoliths composed of calcium carbonate and an organic matrix play a primary role in gravity sensing and the perception of sound. Starmaker (Stm) was the first protein found to be capable of influencing the process of biomineralization of otoliths. Stm dictates the shape, size, and selection of calcium carbonate polymorphs in a concentration-dependent manner. To facilitate exploration of the molecular basis of Stm function, we have developed and optimized a protocol for efficient expression and purification of the homogeneous nontagged Stm. The homogeneous nontagged Stm corresponds to its functional form, which is devoid of a signal peptide. A comprehensive biochemical and biophysical analysis of recombinant Stm, along with in silico examinations, indicate for the first time that Stm exhibits the properties of intrinsically disordered proteins. The functional significance of Stm having intrinsically disordered protein properties and its possible role in controlling the formation of otoliths is discussed.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>18636772</pmid><doi>10.1021/bm800135m</doi><tpages>8</tpages></addata></record> |
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subjects | Animals Biological and medical sciences Biophysics - methods Calcium Carbonate - chemistry Dose-Response Relationship, Drug Fishes Fundamental and applied biological sciences. Psychology Genetic Vectors Molecular biophysics Otolithic Membrane - physiology Protein Conformation Protein Sorting Signals Protein Structure, Tertiary Recombinant Proteins - chemistry Spectrometry, Mass, Electrospray Ionization - methods Spectrophotometry, Ultraviolet - methods Structure in molecular biology Tridimensional structure Zebrafish Zebrafish Proteins - chemistry |
title | Starmaker Exhibits Properties of an Intrinsically Disordered Protein |
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