Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
PROTEIN folding in vivo is mediated by helper proteins, the molecular chaperones 1–3 , of which Hsp60 and its Escherichia coli variant GroEL are some of the best characterized. GroEL is an oligomeric protein with 14 subunits each of M r 60K 4–6 , which possesses weak, co-operative ATPase activity 7–...
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| Veröffentlicht in: | Nature (London) 1994-03, Vol.368 (6468), p.261-265 |
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| creator | Zahn, Ralph Spitzfaden, Claus Ottiger, Marcel Wüthrich, Kurt Plückthun, Andreas |
| description | PROTEIN folding
in vivo
is mediated by helper proteins, the molecular chaperones
1–3
, of which Hsp60 and its
Escherichia coli
variant GroEL are some of the best characterized. GroEL is an oligomeric protein with 14 subunits each of
M
r
60K
4–6
, which possesses weak, co-operative ATPase activity
7–9
> and high plasticity
10
. GroEL seems to interact with non-native proteins, binding one or two molecules per 14-mer
11–19
in a 'central cavity'
20
, but little is known about the conformational state of the bound polypeptides. Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin
21,22
with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. The complete secondary structure of cyclophilin must be disrupted when bound to GroEL. |
| doi_str_mv | 10.1038/368261a0 |
| format | Article |
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in vivo
is mediated by helper proteins, the molecular chaperones
1–3
, of which Hsp60 and its
Escherichia coli
variant GroEL are some of the best characterized. GroEL is an oligomeric protein with 14 subunits each of
M
r
60K
4–6
, which possesses weak, co-operative ATPase activity
7–9
> and high plasticity
10
. GroEL seems to interact with non-native proteins, binding one or two molecules per 14-mer
11–19
in a 'central cavity'
20
, but little is known about the conformational state of the bound polypeptides. Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin
21,22
with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. The complete secondary structure of cyclophilin must be disrupted when bound to GroEL.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/368261a0</identifier><identifier>PMID: 7908413</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Isomerases - chemistry ; Amino Acid Isomerases - metabolism ; Bacteria ; Bacterial Proteins - chemistry ; Biochemistry ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Chaperonin 60 ; Deuterium - chemistry ; E coli ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Heat-Shock Proteins - chemistry ; Humanities and Social Sciences ; Interactions. Associations ; Intermolecular phenomena ; Kinetics ; letter ; Magnetic Resonance Spectroscopy ; Molecular biophysics ; multidisciplinary ; NMR ; Nuclear magnetic resonance ; Peptidylprolyl Isomerase ; Protein Binding ; Protein Denaturation ; Protein Folding ; Protein Structure, Secondary ; Proteins ; Recombinant Proteins - chemistry ; Science ; Science (multidisciplinary) ; Solvents</subject><ispartof>Nature (London), 1994-03, Vol.368 (6468), p.261-265</ispartof><rights>Springer Nature Limited 1994</rights><rights>1994 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Mar 17, 1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c465t-174016434d19385062a5d600abd807d1506325cc72811cba6b3a95d161ef52503</citedby><cites>FETCH-LOGICAL-c465t-174016434d19385062a5d600abd807d1506325cc72811cba6b3a95d161ef52503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/368261a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/368261a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3963876$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7908413$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zahn, Ralph</creatorcontrib><creatorcontrib>Spitzfaden, Claus</creatorcontrib><creatorcontrib>Ottiger, Marcel</creatorcontrib><creatorcontrib>Wüthrich, Kurt</creatorcontrib><creatorcontrib>Plückthun, Andreas</creatorcontrib><title>Destabilization of the complete protein secondary structure on binding to the chaperone GroEL</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>PROTEIN folding
in vivo
is mediated by helper proteins, the molecular chaperones
1–3
, of which Hsp60 and its
Escherichia coli
variant GroEL are some of the best characterized. GroEL is an oligomeric protein with 14 subunits each of
M
r
60K
4–6
, which possesses weak, co-operative ATPase activity
7–9
> and high plasticity
10
. GroEL seems to interact with non-native proteins, binding one or two molecules per 14-mer
11–19
in a 'central cavity'
20
, but little is known about the conformational state of the bound polypeptides. Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin
21,22
with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. The complete secondary structure of cyclophilin must be disrupted when bound to GroEL.</description><subject>Amino Acid Isomerases - chemistry</subject><subject>Amino Acid Isomerases - metabolism</subject><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Chaperonin 60</subject><subject>Deuterium - chemistry</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heat-Shock Proteins - chemistry</subject><subject>Humanities and Social Sciences</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Kinetics</subject><subject>letter</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular biophysics</subject><subject>multidisciplinary</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Peptidylprolyl Isomerase</subject><subject>Protein Binding</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Solvents</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkc1rFTEUxYMo9bUK_gNCECl1MfbmY24yy9IvhQdu7LIMmUymTZmXPJPMQv96I--1Ql24CuT8cnPOPYS8Y_CZgdCnAjVHZuAFWTGpsJGo1UuyAuC6AS3wNTnM-QEAWqbkATlQHWjJxIrcXrhczOBn_8sUHwONEy33jtq42c6uOLpNsTgfaHY2htGknzSXtNiyJEcrPvgw-nBHS9w9uzdbl2Jw9DrFy_Ub8moyc3Zv9-cRubm6_H7-pVl_u_56frZurMS2NNUTMJRCjqwTugXkph0RwAyjBjWyeiN4a63imjE7GByE6dqRIXNTy1sQR-R4N7e6_bHURP3GZ-vm2QQXl9wrrGGR_x9kqDsGoCr44Rn4EJcUaoieg5TYcSErdLKDbIo5Jzf12-Q3dUc9g_5PL_1jLxV9v5-3DBs3PoH7Iqr-ca-bbM08JROsz0-Y6FBohRX7tMNyVcKdS39t_fPlb1epn4c</recordid><startdate>19940317</startdate><enddate>19940317</enddate><creator>Zahn, Ralph</creator><creator>Spitzfaden, Claus</creator><creator>Ottiger, Marcel</creator><creator>Wüthrich, Kurt</creator><creator>Plückthun, Andreas</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>19940317</creationdate><title>Destabilization of the complete protein secondary structure on binding to the chaperone GroEL</title><author>Zahn, Ralph ; Spitzfaden, Claus ; Ottiger, Marcel ; Wüthrich, Kurt ; Plückthun, Andreas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c465t-174016434d19385062a5d600abd807d1506325cc72811cba6b3a95d161ef52503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Isomerases - chemistry</topic><topic>Amino Acid Isomerases - metabolism</topic><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Chaperonin 60</topic><topic>Deuterium - chemistry</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heat-Shock Proteins - chemistry</topic><topic>Humanities and Social Sciences</topic><topic>Interactions. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zahn, Ralph</au><au>Spitzfaden, Claus</au><au>Ottiger, Marcel</au><au>Wüthrich, Kurt</au><au>Plückthun, Andreas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Destabilization of the complete protein secondary structure on binding to the chaperone GroEL</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1994-03-17</date><risdate>1994</risdate><volume>368</volume><issue>6468</issue><spage>261</spage><epage>265</epage><pages>261-265</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>PROTEIN folding
in vivo
is mediated by helper proteins, the molecular chaperones
1–3
, of which Hsp60 and its
Escherichia coli
variant GroEL are some of the best characterized. GroEL is an oligomeric protein with 14 subunits each of
M
r
60K
4–6
, which possesses weak, co-operative ATPase activity
7–9
> and high plasticity
10
. GroEL seems to interact with non-native proteins, binding one or two molecules per 14-mer
11–19
in a 'central cavity'
20
, but little is known about the conformational state of the bound polypeptides. Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin
21,22
with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin. The complete secondary structure of cyclophilin must be disrupted when bound to GroEL.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7908413</pmid><doi>10.1038/368261a0</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1994-03, Vol.368 (6468), p.261-265 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76413620 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Amino Acid Isomerases - chemistry Amino Acid Isomerases - metabolism Bacteria Bacterial Proteins - chemistry Biochemistry Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - metabolism Chaperonin 60 Deuterium - chemistry E coli Escherichia coli Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - chemistry Humanities and Social Sciences Interactions. Associations Intermolecular phenomena Kinetics letter Magnetic Resonance Spectroscopy Molecular biophysics multidisciplinary NMR Nuclear magnetic resonance Peptidylprolyl Isomerase Protein Binding Protein Denaturation Protein Folding Protein Structure, Secondary Proteins Recombinant Proteins - chemistry Science Science (multidisciplinary) Solvents |
| title | Destabilization of the complete protein secondary structure on binding to the chaperone GroEL |
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