Flexible interwoven termini determine the thermal stability of thermosomes
Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperoni...
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| Veröffentlicht in: | Protein & cell 2013-06, Vol.4 (6), p.432-444 |
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| creator | Zhang, Kai Wang, Li Liu, Yanxin Chan, Kwok-Yan Pang, Xiaoyun Schulten, Klaus Dong, Zhiyang Sun, Fei |
| description | Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from
Acidianus tengchongensis
and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes. |
| doi_str_mv | 10.1007/s13238-013-3026-9 |
| format | Article |
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Acidianus tengchongensis
and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.</description><identifier>ISSN: 1674-800X</identifier><identifier>EISSN: 1674-8018</identifier><identifier>DOI: 10.1007/s13238-013-3026-9</identifier><identifier>PMID: 23709365</identifier><language>eng</language><publisher>Beijing: Higher Education Press</publisher><subject>Acidianus - metabolism ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Biochemistry ; Biomedical and Life Sciences ; Cell Biology ; Cryoelectron Microscopy ; Developmental Biology ; Human Genetics ; Hydrogen-Ion Concentration ; Life Sciences ; Molecular Sequence Data ; Mutation ; Nucleotides - metabolism ; Protein Binding ; Protein Folding ; Protein Science ; Protein Stability ; Protein Structure, Quaternary ; Research Article ; Sequence Alignment ; Static Electricity ; Stem Cells ; Temperature ; Thermosomes - chemistry ; Thermosomes - genetics ; Thermosomes - metabolism</subject><ispartof>Protein & cell, 2013-06, Vol.4 (6), p.432-444</ispartof><rights>Higher Education Press and Springer-Verlag Berlin Heidelberg 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-6825a32e38f8c9deff61e6c41d9373bd1b03052b61e6cb85eed81122901bc9373</citedby><cites>FETCH-LOGICAL-c536t-6825a32e38f8c9deff61e6c41d9373bd1b03052b61e6cb85eed81122901bc9373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3740188/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3740188/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,41101,42170,51557,53772,53774</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1007/s13238-013-3026-9$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23709365$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Kai</creatorcontrib><creatorcontrib>Wang, Li</creatorcontrib><creatorcontrib>Liu, Yanxin</creatorcontrib><creatorcontrib>Chan, Kwok-Yan</creatorcontrib><creatorcontrib>Pang, Xiaoyun</creatorcontrib><creatorcontrib>Schulten, Klaus</creatorcontrib><creatorcontrib>Dong, Zhiyang</creatorcontrib><creatorcontrib>Sun, Fei</creatorcontrib><title>Flexible interwoven termini determine the thermal stability of thermosomes</title><title>Protein & cell</title><addtitle>Protein Cell</addtitle><addtitle>Protein Cell</addtitle><description>Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from
Acidianus tengchongensis
and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.</description><subject>Acidianus - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cryoelectron Microscopy</subject><subject>Developmental Biology</subject><subject>Human Genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nucleotides - metabolism</subject><subject>Protein Binding</subject><subject>Protein Folding</subject><subject>Protein Science</subject><subject>Protein Stability</subject><subject>Protein Structure, Quaternary</subject><subject>Research Article</subject><subject>Sequence Alignment</subject><subject>Static Electricity</subject><subject>Stem Cells</subject><subject>Temperature</subject><subject>Thermosomes - chemistry</subject><subject>Thermosomes - genetics</subject><subject>Thermosomes - metabolism</subject><issn>1674-800X</issn><issn>1674-8018</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU1LxDAQhoMorqg_wIsUvHipZpJNml4EEdcPBC8K3kI_prtZ2mZNuqv-e1O7LioYCBkmz7yZyUvIEdAzoDQ598AZVzEFHnPKZJxukT2QyThWFNT2JqYvI3Lo_ZyGxTkImeySEeMJTbkUe-R-UuO7yWuMTNuhe7MrbKMQNKY1UYlDhFE3-9quyerId1luatN9RLYaktbbBv0B2amy2uPh-twnz5Prp6vb-OHx5u7q8iEuBJddLBUTGWfIVaWKtMSqkoCyGEOZ8oTnJeSUU8Hyr2yuBGKpABhLKeRFj-yTi0F3scwbLAtsO5fVeuFMk7kPbTOjf9-0ZqandqV5Mg5fo4LA6VrA2dcl-k43xhdY11mLduk1cBmaZMm4R0_-oHO7dG0YT4MUTAmRUhYoGKjCWe8dVptmgOreLD2YpYNZujdLp6Hm-OcUm4pvawLABsCHq3aK7sfT_6p-AjjfoDI</recordid><startdate>20130601</startdate><enddate>20130601</enddate><creator>Zhang, Kai</creator><creator>Wang, Li</creator><creator>Liu, Yanxin</creator><creator>Chan, Kwok-Yan</creator><creator>Pang, Xiaoyun</creator><creator>Schulten, Klaus</creator><creator>Dong, Zhiyang</creator><creator>Sun, Fei</creator><general>Higher Education Press</general><general>Springer Nature B.V</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130601</creationdate><title>Flexible interwoven termini determine the thermal stability of thermosomes</title><author>Zhang, Kai ; Wang, Li ; Liu, Yanxin ; Chan, Kwok-Yan ; Pang, Xiaoyun ; Schulten, Klaus ; Dong, Zhiyang ; Sun, Fei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-6825a32e38f8c9deff61e6c41d9373bd1b03052b61e6cb85eed81122901bc9373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acidianus - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Cryoelectron Microscopy</topic><topic>Developmental Biology</topic><topic>Human Genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Nucleotides - metabolism</topic><topic>Protein Binding</topic><topic>Protein Folding</topic><topic>Protein Science</topic><topic>Protein Stability</topic><topic>Protein Structure, Quaternary</topic><topic>Research Article</topic><topic>Sequence Alignment</topic><topic>Static Electricity</topic><topic>Stem Cells</topic><topic>Temperature</topic><topic>Thermosomes - chemistry</topic><topic>Thermosomes - genetics</topic><topic>Thermosomes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Kai</creatorcontrib><creatorcontrib>Wang, Li</creatorcontrib><creatorcontrib>Liu, Yanxin</creatorcontrib><creatorcontrib>Chan, Kwok-Yan</creatorcontrib><creatorcontrib>Pang, Xiaoyun</creatorcontrib><creatorcontrib>Schulten, Klaus</creatorcontrib><creatorcontrib>Dong, Zhiyang</creatorcontrib><creatorcontrib>Sun, Fei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein & cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Zhang, Kai</au><au>Wang, Li</au><au>Liu, Yanxin</au><au>Chan, Kwok-Yan</au><au>Pang, Xiaoyun</au><au>Schulten, Klaus</au><au>Dong, Zhiyang</au><au>Sun, Fei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Flexible interwoven termini determine the thermal stability of thermosomes</atitle><jtitle>Protein & cell</jtitle><stitle>Protein Cell</stitle><addtitle>Protein Cell</addtitle><date>2013-06-01</date><risdate>2013</risdate><volume>4</volume><issue>6</issue><spage>432</spage><epage>444</epage><pages>432-444</pages><issn>1674-800X</issn><eissn>1674-8018</eissn><abstract>Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from
Acidianus tengchongensis
and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.</abstract><cop>Beijing</cop><pub>Higher Education Press</pub><pmid>23709365</pmid><doi>10.1007/s13238-013-3026-9</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Protein & cell, 2013-06, Vol.4 (6), p.432-444 |
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| language | eng |
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| subjects | Acidianus - metabolism Adenosine Triphosphate - metabolism Amino Acid Sequence Biochemistry Biomedical and Life Sciences Cell Biology Cryoelectron Microscopy Developmental Biology Human Genetics Hydrogen-Ion Concentration Life Sciences Molecular Sequence Data Mutation Nucleotides - metabolism Protein Binding Protein Folding Protein Science Protein Stability Protein Structure, Quaternary Research Article Sequence Alignment Static Electricity Stem Cells Temperature Thermosomes - chemistry Thermosomes - genetics Thermosomes - metabolism |
| title | Flexible interwoven termini determine the thermal stability of thermosomes |
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