Discovery of an intermolecular disulfide bond required for the thermostability of a heterodimeric protein from the thermophile Hydrogenobacter thermophilus
Factors that increase protein thermostability are of considerable interest in both scientific and industrial fields. Disulfide bonds are one of such factors that increase thermostability, but are rarely found in intracellular proteins because of the reducing environment of the cytosol. Here, we repo...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2016-02, Vol.80 (2), p.232-240 |
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| creator | Kim, Keug Tae Chiba, Yoko Arai, Hiroyuki Ishii, Masaharu |
| description | Factors that increase protein thermostability are of considerable interest in both scientific and industrial fields. Disulfide bonds are one of such factors that increase thermostability, but are rarely found in intracellular proteins because of the reducing environment of the cytosol. Here, we report the first example of an intermolecular disulfide bond between heteromeric subunits of a novel-type phosphoserine phosphatase from a thermophilic bacterium Hydrogenobacter thermophilus, which contributes to the protein thermostability at the physiological temperature. Comparison of remaining soluble proteins between wild-type and cysteine-deleted mutant using SDS-PAGE revealed that the disulfide bond increases the thermostability of the whole protein by tightly connecting a subunit with low solubility to the partner with higher solubility. Furthermore, it was strongly suggested that the disulfide bond is formed and contributes to the stability in vivo. This finding will open new avenues for the design of proteins with increased thermostability.
Intermolecular disulfide bond was found in a heterodimeric protein from a thermophilic bacterium. It is essential for the protein thermostability. |
| doi_str_mv | 10.1080/09168451.2015.1079476 |
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Intermolecular disulfide bond was found in a heterodimeric protein from a thermophilic bacterium. It is essential for the protein thermostability.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2015.1079476</identifier><identifier>PMID: 26360333</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>Bacteria - chemistry ; Bacteria - enzymology ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Disulfides - chemistry ; Enzyme Stability ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Gene Expression ; heterodimer ; Hot Temperature ; intermolecular disulfide bond ; Mutation ; Phosphoric Monoester Hydrolases - chemistry ; Phosphoric Monoester Hydrolases - genetics ; Phosphoric Monoester Hydrolases - metabolism ; phosphoserine phosphatase ; Protein Multimerization ; protein solubility ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; protein thermostability ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Solubility</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2016-02, Vol.80 (2), p.232-240</ispartof><rights>2015 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c547t-809e864d65ec3f0edb5ed3c7ddeea8e4c2431fede674889f03c75a789a9a12fc3</citedby><cites>FETCH-LOGICAL-c547t-809e864d65ec3f0edb5ed3c7ddeea8e4c2431fede674889f03c75a789a9a12fc3</cites><orcidid>0000-0002-2734-0836</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26360333$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Keug Tae</creatorcontrib><creatorcontrib>Chiba, Yoko</creatorcontrib><creatorcontrib>Arai, Hiroyuki</creatorcontrib><creatorcontrib>Ishii, Masaharu</creatorcontrib><title>Discovery of an intermolecular disulfide bond required for the thermostability of a heterodimeric protein from the thermophile Hydrogenobacter thermophilus</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Factors that increase protein thermostability are of considerable interest in both scientific and industrial fields. Disulfide bonds are one of such factors that increase thermostability, but are rarely found in intracellular proteins because of the reducing environment of the cytosol. Here, we report the first example of an intermolecular disulfide bond between heteromeric subunits of a novel-type phosphoserine phosphatase from a thermophilic bacterium Hydrogenobacter thermophilus, which contributes to the protein thermostability at the physiological temperature. Comparison of remaining soluble proteins between wild-type and cysteine-deleted mutant using SDS-PAGE revealed that the disulfide bond increases the thermostability of the whole protein by tightly connecting a subunit with low solubility to the partner with higher solubility. Furthermore, it was strongly suggested that the disulfide bond is formed and contributes to the stability in vivo. This finding will open new avenues for the design of proteins with increased thermostability.
Intermolecular disulfide bond was found in a heterodimeric protein from a thermophilic bacterium. It is essential for the protein thermostability.</description><subject>Bacteria - chemistry</subject><subject>Bacteria - enzymology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Disulfides - chemistry</subject><subject>Enzyme Stability</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Gene Expression</subject><subject>heterodimer</subject><subject>Hot Temperature</subject><subject>intermolecular disulfide bond</subject><subject>Mutation</subject><subject>Phosphoric Monoester Hydrolases - chemistry</subject><subject>Phosphoric Monoester Hydrolases - genetics</subject><subject>Phosphoric Monoester Hydrolases - metabolism</subject><subject>phosphoserine phosphatase</subject><subject>Protein Multimerization</subject><subject>protein solubility</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>protein thermostability</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Solubility</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFu1DAQhi1ERZfCI4B85JJir2PHuYFaoEiVemnPlmOPWSMn3o4T0D4LL4uj3aKeOFiWZ77_H2t-Qt5xdsmZZh9Zz5VuJb_cMi5rqevbTr0gGy7arlH18ZJsVqZZoXPyupSfjNWC5K_I-VYJxYQQG_LnOhaXfwEeaA7UTjROM-CYE7glWaQ-liWF6IEOefIU4XGJCJ6GjHTewXoqXWY7xBTnowndQfXIPo6A0dE95hniRAPm8Zlmv4sJ6M3BY_4BUx6sq6JnvaW8IWfBpgJvT_cFefj65f7qprm9-_b96vNt42TbzY1mPWjVeiXBicDADxK8cJ33AFZD67at4AE8qK7Vug-s9qTtdG97y7fBiQvy4ehbf_q4QJnNWJcCKdkJ8lIM7xSrA4TUFZVH1GEuBSGYPcbR4sFwZtZczFMuZs3FnHKpuvenEcswgv-negqiAp-OQJzqakf7O2PyZraHlDGgnVwsRvx_xl_zm6Jt</recordid><startdate>20160201</startdate><enddate>20160201</enddate><creator>Kim, Keug Tae</creator><creator>Chiba, Yoko</creator><creator>Arai, Hiroyuki</creator><creator>Ishii, Masaharu</creator><general>Taylor & Francis</general><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><orcidid>https://orcid.org/0000-0002-2734-0836</orcidid></search><sort><creationdate>20160201</creationdate><title>Discovery of an intermolecular disulfide bond required for the thermostability of a heterodimeric protein from the thermophile Hydrogenobacter thermophilus</title><author>Kim, Keug Tae ; Chiba, Yoko ; Arai, Hiroyuki ; Ishii, Masaharu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c547t-809e864d65ec3f0edb5ed3c7ddeea8e4c2431fede674889f03c75a789a9a12fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Bacteria - chemistry</topic><topic>Bacteria - enzymology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Disulfides - chemistry</topic><topic>Enzyme Stability</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Gene Expression</topic><topic>heterodimer</topic><topic>Hot Temperature</topic><topic>intermolecular disulfide bond</topic><topic>Mutation</topic><topic>Phosphoric Monoester Hydrolases - chemistry</topic><topic>Phosphoric Monoester Hydrolases - genetics</topic><topic>Phosphoric Monoester Hydrolases - metabolism</topic><topic>phosphoserine phosphatase</topic><topic>Protein Multimerization</topic><topic>protein solubility</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>protein thermostability</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Keug Tae</creatorcontrib><creatorcontrib>Chiba, Yoko</creatorcontrib><creatorcontrib>Arai, Hiroyuki</creatorcontrib><creatorcontrib>Ishii, Masaharu</creatorcontrib><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><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Keug Tae</au><au>Chiba, Yoko</au><au>Arai, Hiroyuki</au><au>Ishii, Masaharu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Discovery of an intermolecular disulfide bond required for the thermostability of a heterodimeric protein from the thermophile Hydrogenobacter thermophilus</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2016-02-01</date><risdate>2016</risdate><volume>80</volume><issue>2</issue><spage>232</spage><epage>240</epage><pages>232-240</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Factors that increase protein thermostability are of considerable interest in both scientific and industrial fields. Disulfide bonds are one of such factors that increase thermostability, but are rarely found in intracellular proteins because of the reducing environment of the cytosol. Here, we report the first example of an intermolecular disulfide bond between heteromeric subunits of a novel-type phosphoserine phosphatase from a thermophilic bacterium Hydrogenobacter thermophilus, which contributes to the protein thermostability at the physiological temperature. Comparison of remaining soluble proteins between wild-type and cysteine-deleted mutant using SDS-PAGE revealed that the disulfide bond increases the thermostability of the whole protein by tightly connecting a subunit with low solubility to the partner with higher solubility. Furthermore, it was strongly suggested that the disulfide bond is formed and contributes to the stability in vivo. This finding will open new avenues for the design of proteins with increased thermostability.
Intermolecular disulfide bond was found in a heterodimeric protein from a thermophilic bacterium. It is essential for the protein thermostability.</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>26360333</pmid><doi>10.1080/09168451.2015.1079476</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-2734-0836</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Freely Accessible Japanese Titles; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Bacteria - chemistry Bacteria - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Disulfides - chemistry Enzyme Stability Escherichia coli - genetics Escherichia coli - metabolism Gene Expression heterodimer Hot Temperature intermolecular disulfide bond Mutation Phosphoric Monoester Hydrolases - chemistry Phosphoric Monoester Hydrolases - genetics Phosphoric Monoester Hydrolases - metabolism phosphoserine phosphatase Protein Multimerization protein solubility Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism protein thermostability Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Solubility |
| title | Discovery of an intermolecular disulfide bond required for the thermostability of a heterodimeric protein from the thermophile Hydrogenobacter thermophilus |
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