Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechan...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2000-08, Vol.289 (5483), p.1317-1321 |
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| creator | Serio, Tricia R. Cashikar, Anil G. Kowal, Anthony S. Sawicki, George J. Moslehi, Jahan J. Serpell, Louise Arnsdorf, Morton F. Lindquist, Susan L. |
| description | Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes. |
| doi_str_mv | 10.1126/science.289.5483.1317 |
| format | Article |
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The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.289.5483.1317</identifier><identifier>PMID: 10958771</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>amyloid ; Amyloid - chemistry ; Amyloids ; Biological and medical sciences ; Biopolymers - chemistry ; Brain chemistry ; Cellular biology ; Centrifugation, Density Gradient ; Circular Dichroism ; Degeneration ; Diseases ; Electrophoresis, Polyacrylamide Gel ; Endopeptidases - metabolism ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - metabolism ; Fungal Proteins - ultrastructure ; Genetics ; Heinrich events ; Kinetics ; Light ; Light scattering ; Micelles ; Microscopy, Atomic Force ; Microscopy, Electron ; Models, Chemical ; Molecular and cellular biology ; Molecular genetics ; Monomers ; Nerve degeneration ; Nervous system ; Neurons ; Nucleation ; Oligomers ; Paleoclimatology ; Peptide Termination Factors ; Polymerization ; Prions ; Prions - chemistry ; Prions - metabolism ; Prions - ultrastructure ; Protein Conformation ; Protein Folding ; Proteins ; Replication ; Research Article ; Saccharomyces cerevisiae Proteins ; Scattering, Radiation ; Sediments ; Solubility ; Sonication ; Sup35 protein</subject><ispartof>Science (American Association for the Advancement of Science), 2000-08, Vol.289 (5483), p.1317-1321</ispartof><rights>Copyright 2000 American Association for the Advancement of Science</rights><rights>2000 INIST-CNRS</rights><rights>COPYRIGHT 2000 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2000 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Aug 25, 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c786t-8f3815de86e71d909ab5f18bef56ede57e51c49ced79520ce567734f733b71b43</citedby><cites>FETCH-LOGICAL-c786t-8f3815de86e71d909ab5f18bef56ede57e51c49ced79520ce567734f733b71b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3077621$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3077621$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1536206$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10958771$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serio, Tricia R.</creatorcontrib><creatorcontrib>Cashikar, Anil G.</creatorcontrib><creatorcontrib>Kowal, Anthony S.</creatorcontrib><creatorcontrib>Sawicki, George J.</creatorcontrib><creatorcontrib>Moslehi, Jahan J.</creatorcontrib><creatorcontrib>Serpell, Louise</creatorcontrib><creatorcontrib>Arnsdorf, Morton F.</creatorcontrib><creatorcontrib>Lindquist, Susan L.</creatorcontrib><title>Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.</description><subject>amyloid</subject><subject>Amyloid - chemistry</subject><subject>Amyloids</subject><subject>Biological and medical sciences</subject><subject>Biopolymers - chemistry</subject><subject>Brain chemistry</subject><subject>Cellular biology</subject><subject>Centrifugation, Density Gradient</subject><subject>Circular Dichroism</subject><subject>Degeneration</subject><subject>Diseases</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidases - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungal Proteins - ultrastructure</subject><subject>Genetics</subject><subject>Heinrich events</subject><subject>Kinetics</subject><subject>Light</subject><subject>Light scattering</subject><subject>Micelles</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron</subject><subject>Models, Chemical</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Monomers</subject><subject>Nerve degeneration</subject><subject>Nervous system</subject><subject>Neurons</subject><subject>Nucleation</subject><subject>Oligomers</subject><subject>Paleoclimatology</subject><subject>Peptide Termination Factors</subject><subject>Polymerization</subject><subject>Prions</subject><subject>Prions - chemistry</subject><subject>Prions - metabolism</subject><subject>Prions - ultrastructure</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Replication</subject><subject>Research Article</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Scattering, Radiation</subject><subject>Sediments</subject><subject>Solubility</subject><subject>Sonication</subject><subject>Sup35 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Conformational Conversion and the Replication of Conformational Information by a Prion Determinant</title><author>Serio, Tricia R. ; Cashikar, Anil G. ; Kowal, Anthony S. ; Sawicki, George J. ; Moslehi, Jahan J. ; Serpell, Louise ; Arnsdorf, Morton F. ; Lindquist, Susan L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c786t-8f3815de86e71d909ab5f18bef56ede57e51c49ced79520ce567734f733b71b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>amyloid</topic><topic>Amyloid - chemistry</topic><topic>Amyloids</topic><topic>Biological and medical sciences</topic><topic>Biopolymers - chemistry</topic><topic>Brain chemistry</topic><topic>Cellular biology</topic><topic>Centrifugation, Density Gradient</topic><topic>Circular Dichroism</topic><topic>Degeneration</topic><topic>Diseases</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidases - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungal Proteins - ultrastructure</topic><topic>Genetics</topic><topic>Heinrich events</topic><topic>Kinetics</topic><topic>Light</topic><topic>Light scattering</topic><topic>Micelles</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Electron</topic><topic>Models, Chemical</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Monomers</topic><topic>Nerve degeneration</topic><topic>Nervous system</topic><topic>Neurons</topic><topic>Nucleation</topic><topic>Oligomers</topic><topic>Paleoclimatology</topic><topic>Peptide Termination Factors</topic><topic>Polymerization</topic><topic>Prions</topic><topic>Prions - chemistry</topic><topic>Prions - metabolism</topic><topic>Prions - ultrastructure</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Replication</topic><topic>Research 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Science)</jtitle><addtitle>Science</addtitle><date>2000-08-25</date><risdate>2000</risdate><volume>289</volume><issue>5483</issue><spage>1317</spage><epage>1321</epage><pages>1317-1321</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>10958771</pmid><doi>10.1126/science.289.5483.1317</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2000-08, Vol.289 (5483), p.1317-1321 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743314301 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | amyloid Amyloid - chemistry Amyloids Biological and medical sciences Biopolymers - chemistry Brain chemistry Cellular biology Centrifugation, Density Gradient Circular Dichroism Degeneration Diseases Electrophoresis, Polyacrylamide Gel Endopeptidases - metabolism Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - metabolism Fungal Proteins - ultrastructure Genetics Heinrich events Kinetics Light Light scattering Micelles Microscopy, Atomic Force Microscopy, Electron Models, Chemical Molecular and cellular biology Molecular genetics Monomers Nerve degeneration Nervous system Neurons Nucleation Oligomers Paleoclimatology Peptide Termination Factors Polymerization Prions Prions - chemistry Prions - metabolism Prions - ultrastructure Protein Conformation Protein Folding Proteins Replication Research Article Saccharomyces cerevisiae Proteins Scattering, Radiation Sediments Solubility Sonication Sup35 protein |
| title | Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant |
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