Chaperonin Function: Folding by Forced Unfolding
The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required fo...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1999-04, Vol.284 (5415), p.822-825 |
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| creator | Shtilerman, Mark Lorimer, George H. Englander, S. Walter |
| description | The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding. |
| doi_str_mv | 10.1126/science.284.5415.822 |
| format | Article |
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Walter</creator><creatorcontrib>Shtilerman, Mark ; Lorimer, George H. ; Englander, S. Walter</creatorcontrib><description>The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.284.5415.822</identifier><identifier>PMID: 10221918</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Adenosine Triphosphate - metabolism ; Adenylyl Imidodiphosphate - metabolism ; Amides ; Analytical, structural and metabolic biochemistry ; Binding and carrier proteins ; Binding Sites ; Biochemistry ; Biological and medical sciences ; Chaperonin 10 - chemistry ; Chaperonin 10 - metabolism ; Chaperonin 10 - physiology ; Chaperonin 60 - chemistry ; Chaperonin 60 - metabolism ; Chaperonin 60 - physiology ; Chaperonins ; Denaturation ; Fundamental and applied biological sciences. Psychology ; Hydrogen ; Hydrogen - chemistry ; Hydrogen - metabolism ; Hydrolysis ; Models, Molecular ; Molecules ; Protein Binding ; Protein Conformation ; Protein denaturation ; Protein Folding ; Protein Structure, Secondary ; Protein unfolding ; Proteins ; Rhodosphirillium rubrum ; Ribulose-Bisphosphate Carboxylase - chemistry ; Ribulose-Bisphosphate Carboxylase - metabolism ; Tritium</subject><ispartof>Science (American Association for the Advancement of Science), 1999-04, Vol.284 (5415), p.822-825</ispartof><rights>Copyright 1999 American Association for the Advancement of Science</rights><rights>1999 INIST-CNRS</rights><rights>COPYRIGHT 1999 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1999 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c825t-b78beff39083586387b3299b8b083bf935deb3fb42fa3d00b364fbadf04569673</citedby><cites>FETCH-LOGICAL-c825t-b78beff39083586387b3299b8b083bf935deb3fb42fa3d00b364fbadf04569673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2898324$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2898324$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,780,784,803,885,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1786959$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10221918$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shtilerman, Mark</creatorcontrib><creatorcontrib>Lorimer, George H.</creatorcontrib><creatorcontrib>Englander, S. Walter</creatorcontrib><title>Chaperonin Function: Folding by Forced Unfolding</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Adenylyl Imidodiphosphate - metabolism</subject><subject>Amides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding and carrier proteins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chaperonin 10 - chemistry</subject><subject>Chaperonin 10 - metabolism</subject><subject>Chaperonin 10 - physiology</subject><subject>Chaperonin 60 - chemistry</subject><subject>Chaperonin 60 - metabolism</subject><subject>Chaperonin 60 - physiology</subject><subject>Chaperonins</subject><subject>Denaturation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen</subject><subject>Hydrogen - chemistry</subject><subject>Hydrogen - metabolism</subject><subject>Hydrolysis</subject><subject>Models, Molecular</subject><subject>Molecules</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein denaturation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein unfolding</subject><subject>Proteins</subject><subject>Rhodosphirillium rubrum</subject><subject>Ribulose-Bisphosphate Carboxylase - chemistry</subject><subject>Ribulose-Bisphosphate Carboxylase - metabolism</subject><subject>Tritium</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0k1r2zAYB3AxNtYs2zcoI4cxdqgzvdrSDoM2LFkhLIetuwpJllwVR0otZ7TffgoOXQOBBR9snuenR0j-A3CO4BQhXH5Oxttg7BRzOmUUsSnH-AUYIShYITAkL8EIQlIWHFbsDLxJ6Q7C3BPkNThDEGMkEB8BOLtVG9vF4MNkvg2m9zF8mcxjW_vQTPRj_uyMrSc3wQ21t-CVU22y7_bvMbiZf_s1-14sV4vr2eWyMByzvtAV19Y5IiAnjJeEV5pgITTXuaCdIKy2mjhNsVOkhlCTkjqtagcpK0VZkTH4OszdbPXa1saGvlOt3HR-rbpHGZWXh53gb2UT_0hCcVUynAd83A_o4v3Wpl6ufTK2bVWwcZtkKSqMqKD_hajKl8UQyvBigI1qrfT5RvLGprHB5v1jsM7n8iWjZT4xZpkXR3h-arv25pj_dOAz6e1D36htSvL654-T6er3yfRqcSrli-UBvThGTWxb21iZkzBbHXA6cNPFlDrrnv4jgnKXZrlPs8xplrs0y5zmvOz98ww8WzTEN4MPe6CSUa3rVDA-_XMVL3eJH4Pzgd2lPnZPbcwFJ5iSv_tFA0I</recordid><startdate>19990430</startdate><enddate>19990430</enddate><creator>Shtilerman, Mark</creator><creator>Lorimer, George H.</creator><creator>Englander, S. Walter</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19990430</creationdate><title>Chaperonin Function: Folding by Forced Unfolding</title><author>Shtilerman, Mark ; Lorimer, George H. ; Englander, S. Walter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c825t-b78beff39083586387b3299b8b083bf935deb3fb42fa3d00b364fbadf04569673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Adenylyl Imidodiphosphate - metabolism</topic><topic>Amides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding and carrier proteins</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chaperonin 10 - chemistry</topic><topic>Chaperonin 10 - metabolism</topic><topic>Chaperonin 10 - physiology</topic><topic>Chaperonin 60 - chemistry</topic><topic>Chaperonin 60 - metabolism</topic><topic>Chaperonin 60 - physiology</topic><topic>Chaperonins</topic><topic>Denaturation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen</topic><topic>Hydrogen - chemistry</topic><topic>Hydrogen - metabolism</topic><topic>Hydrolysis</topic><topic>Models, Molecular</topic><topic>Molecules</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein denaturation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein unfolding</topic><topic>Proteins</topic><topic>Rhodosphirillium rubrum</topic><topic>Ribulose-Bisphosphate Carboxylase - chemistry</topic><topic>Ribulose-Bisphosphate Carboxylase - metabolism</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shtilerman, Mark</creatorcontrib><creatorcontrib>Lorimer, George H.</creatorcontrib><creatorcontrib>Englander, S. 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Walter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chaperonin Function: Folding by Forced Unfolding</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1999-04-30</date><risdate>1999</risdate><volume>284</volume><issue>5415</issue><spage>822</spage><epage>825</epage><pages>822-825</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is only partial, requires the complete chaperonin system, and is accomplished within the 13 seconds required for a single system turnover. The binding of nucleoside triphosphate provides the energy for a single unfolding event; multiple turnovers require adenosine triphosphate hydrolysis. The substrate protein is released on each turnover even if it has not yet refolded to the native state. These results suggest that GroEL helps partly folded but blocked proteins to fold by causing them first to partially unfold. The structure of GroEL seems well suited to generate the nonspecific mechanical stretching force required for forceful protein unfolding.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>10221918</pmid><doi>10.1126/science.284.5415.822</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 1999-04, Vol.284 (5415), p.822-825 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Adenosine Triphosphate - metabolism Adenylyl Imidodiphosphate - metabolism Amides Analytical, structural and metabolic biochemistry Binding and carrier proteins Binding Sites Biochemistry Biological and medical sciences Chaperonin 10 - chemistry Chaperonin 10 - metabolism Chaperonin 10 - physiology Chaperonin 60 - chemistry Chaperonin 60 - metabolism Chaperonin 60 - physiology Chaperonins Denaturation Fundamental and applied biological sciences. Psychology Hydrogen Hydrogen - chemistry Hydrogen - metabolism Hydrolysis Models, Molecular Molecules Protein Binding Protein Conformation Protein denaturation Protein Folding Protein Structure, Secondary Protein unfolding Proteins Rhodosphirillium rubrum Ribulose-Bisphosphate Carboxylase - chemistry Ribulose-Bisphosphate Carboxylase - metabolism Tritium |
| title | Chaperonin Function: Folding by Forced Unfolding |
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