Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8
sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggr...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2010, Vol.74 (8), p.1556-1563 |
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| creator | HOSSAIN, MD. Tofazzal TESHIBA, Satoshi SHIGEOKA, Yuichi FUJISAWA, Tetsuro INOKO, Yoji SAKANO, Daisuke YAMAMOTO, Kohji BANNO, Yutaka ASO, Yoichi |
| description | sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling. |
| doi_str_mv | 10.1271/bbb.100131 |
| format | Article |
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Tofazzal ; TESHIBA, Satoshi ; SHIGEOKA, Yuichi ; FUJISAWA, Tetsuro ; INOKO, Yoji ; SAKANO, Daisuke ; YAMAMOTO, Kohji ; BANNO, Yutaka ; ASO, Yoichi</creator><creatorcontrib>HOSSAIN, MD. Tofazzal ; TESHIBA, Satoshi ; SHIGEOKA, Yuichi ; FUJISAWA, Tetsuro ; INOKO, Yoji ; SAKANO, Daisuke ; YAMAMOTO, Kohji ; BANNO, Yutaka ; ASO, Yoichi</creatorcontrib><description>sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.</description><identifier>ISSN: 0916-8451</identifier><identifier>ISSN: 1347-6947</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.100131</identifier><identifier>PMID: 20699588</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>aggregation ; Animals ; Biological and medical sciences ; Bombyx ; Bombyx mori ; Fundamental and applied biological sciences. Psychology ; Heat-Shock Proteins, Small - chemistry ; Heat-Shock Proteins, Small - metabolism ; Insect Proteins - chemistry ; Insect Proteins - metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Scattering, Small Angle ; silkworm ; small heat-shock protein ; Temperature ; X-Ray Diffraction</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2010, Vol.74 (8), p.1556-1563</ispartof><rights>2010 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c667t-7aa48a35517b1649caa129c708c5c72e0ff17a0c55ae56aef5218ef4801471cb3</citedby><cites>FETCH-LOGICAL-c667t-7aa48a35517b1649caa129c708c5c72e0ff17a0c55ae56aef5218ef4801471cb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4022,27922,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23378070$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20699588$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HOSSAIN, MD. Tofazzal</creatorcontrib><creatorcontrib>TESHIBA, Satoshi</creatorcontrib><creatorcontrib>SHIGEOKA, Yuichi</creatorcontrib><creatorcontrib>FUJISAWA, Tetsuro</creatorcontrib><creatorcontrib>INOKO, Yoji</creatorcontrib><creatorcontrib>SAKANO, Daisuke</creatorcontrib><creatorcontrib>YAMAMOTO, Kohji</creatorcontrib><creatorcontrib>BANNO, Yutaka</creatorcontrib><creatorcontrib>ASO, Yoichi</creatorcontrib><title>Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.</description><subject>aggregation</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bombyx</subject><subject>Bombyx mori</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heat-Shock Proteins, Small - chemistry</subject><subject>Heat-Shock Proteins, Small - metabolism</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - metabolism</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Quaternary</subject><subject>Scattering, Small Angle</subject><subject>silkworm</subject><subject>small heat-shock protein</subject><subject>Temperature</subject><subject>X-Ray Diffraction</subject><issn>0916-8451</issn><issn>1347-6947</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1LwzAYwPEgis6Xix9AehFB6MzTJk3iTYY6QXBYPZenWYLVtJ1Ji-zb27mpF8FTSPglefgTcgx0DImAi7Isx0AppLBFRpAyEWeKiW0yogqyWDIOe2Q_hFdKhwMOu2QvoZlSXMoRecw73-uu9-iimW8XxneVCVFro7xybx-tr6O8RueiqcEuzl9a_bZynamacBmFaT4DNVYRNvOvTULH8pDsWHTBHG3WA_J8c_00mcb3D7d3k6v7WGeZ6GKByCSmnIMoIWNKI0KitKBScy0SQ60FgVRzjoZnaCxPQBrLJAUmQJfpATlbv7vw7XtvQlfUVdDGOWxM24dCAucMlKL_SsGkkpIKMcjztdS-DcEbWyx8VaNfFkCLVexiiF2sYw_4ZPNsX9Zm_kO_6w7gdAMwaHTWY6Or8OvSVAy_rubja1c1diiOQ3Y3LzpcutZ_X0r_GOATtuuWWw</recordid><startdate>2010</startdate><enddate>2010</enddate><creator>HOSSAIN, MD. Tofazzal</creator><creator>TESHIBA, Satoshi</creator><creator>SHIGEOKA, Yuichi</creator><creator>FUJISAWA, Tetsuro</creator><creator>INOKO, Yoji</creator><creator>SAKANO, Daisuke</creator><creator>YAMAMOTO, Kohji</creator><creator>BANNO, Yutaka</creator><creator>ASO, Yoichi</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2010</creationdate><title>Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8</title><author>HOSSAIN, MD. Tofazzal ; TESHIBA, Satoshi ; SHIGEOKA, Yuichi ; FUJISAWA, Tetsuro ; INOKO, Yoji ; SAKANO, Daisuke ; YAMAMOTO, Kohji ; BANNO, Yutaka ; ASO, Yoichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c667t-7aa48a35517b1649caa129c708c5c72e0ff17a0c55ae56aef5218ef4801471cb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>aggregation</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bombyx</topic><topic>Bombyx mori</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heat-Shock Proteins, Small - chemistry</topic><topic>Heat-Shock Proteins, Small - metabolism</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - metabolism</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Quaternary</topic><topic>Scattering, Small Angle</topic><topic>silkworm</topic><topic>small heat-shock protein</topic><topic>Temperature</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HOSSAIN, MD. Tofazzal</creatorcontrib><creatorcontrib>TESHIBA, Satoshi</creatorcontrib><creatorcontrib>SHIGEOKA, Yuichi</creatorcontrib><creatorcontrib>FUJISAWA, Tetsuro</creatorcontrib><creatorcontrib>INOKO, Yoji</creatorcontrib><creatorcontrib>SAKANO, Daisuke</creatorcontrib><creatorcontrib>YAMAMOTO, Kohji</creatorcontrib><creatorcontrib>BANNO, Yutaka</creatorcontrib><creatorcontrib>ASO, Yoichi</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>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HOSSAIN, MD. Tofazzal</au><au>TESHIBA, Satoshi</au><au>SHIGEOKA, Yuichi</au><au>FUJISAWA, Tetsuro</au><au>INOKO, Yoji</au><au>SAKANO, Daisuke</au><au>YAMAMOTO, Kohji</au><au>BANNO, Yutaka</au><au>ASO, Yoichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2010</date><risdate>2010</risdate><volume>74</volume><issue>8</issue><spage>1556</spage><epage>1563</epage><pages>1556-1563</pages><issn>0916-8451</issn><issn>1347-6947</issn><eissn>1347-6947</eissn><abstract>sHSP20.8 and sHSP19.9 are silkworm small-heat shock proteins (sHSPs) comprising a number of polypeptides of molecular sizes of several tens of kilodaltons as subunits. The structural properties of sHSPs were investigated. sHSP19.9 was found to be aggregated by itself during incubation at 60 °C. Aggregation was suppressed in the presence of dithiothreitol and at high ionic strength. In contrast, sHSP20.8 was not aggregated. Aggregation of sHSP19.9 was partially suppressed by sHSP20.8 and in the presence of catalase as a target protein. Based on changes in small-angle X-ray scattering, it is possible that the molecular size of sHSP19.9 is larger than that of sHSP20.8, and that their molecular sizes increase with increasing temperature in a reversible, biphasic manner. sHSPs did not protect catalase from thermal inactivation, but protected it from precipitation by forming a soluble complex. sHSP20.8 and sHSP19.9 with dithiothreitol were stable against lyophilization, autoclaving at 120 °C, and boiling.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>20699588</pmid><doi>10.1271/bbb.100131</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; Free Full-Text Journals in Chemistry |
| subjects | aggregation Animals Biological and medical sciences Bombyx Bombyx mori Fundamental and applied biological sciences. Psychology Heat-Shock Proteins, Small - chemistry Heat-Shock Proteins, Small - metabolism Insect Proteins - chemistry Insect Proteins - metabolism Protein Multimerization Protein Structure, Quaternary Scattering, Small Angle silkworm small heat-shock protein Temperature X-Ray Diffraction |
| title | Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8 |
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