Interactions between non-identical prion proteins

Prion formation involves the conversion of soluble proteins into an infectious amyloid form. This process is highly specific, with prion aggregates templating the conversion of identical proteins. However, in some cases non-identical prion proteins can interact to promote or inhibit prion formation...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Seminars in cell & developmental biology 2011-07, Vol.22 (5), p.437-443
Hauptverfasser: Gonzalez Nelson, Aaron C., Ross, Eric D.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 443
container_issue 5
container_start_page 437
container_title Seminars in cell & developmental biology
container_volume 22
creator Gonzalez Nelson, Aaron C.
Ross, Eric D.
description Prion formation involves the conversion of soluble proteins into an infectious amyloid form. This process is highly specific, with prion aggregates templating the conversion of identical proteins. However, in some cases non-identical prion proteins can interact to promote or inhibit prion formation or propagation. These interactions affect both the efficiency with which prion diseases are transmitted across species and the normal physiology of yeast prion formation and propagation. Here we examine two types of heterologous prion interactions: interactions between related proteins from different species (the species barrier) and interactions between unrelated prion proteins within a single species. Interestingly, although very subtle changes in protein sequence can significantly reduce or eliminate cross-species prion transmission, in Saccharomyces cerevisiae completely unrelated prion proteins can interact to affect prion formation and propagation.
doi_str_mv 10.1016/j.semcdb.2011.02.022
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_911154486</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1084952111000358</els_id><sourcerecordid>911154486</sourcerecordid><originalsourceid>FETCH-LOGICAL-c393t-70c56ca3fd8c4ab4aa33ad55558fd16dc69d6ea8cbba61e5ab32600e1dd554113</originalsourceid><addsrcrecordid>eNqFkE1LxDAQhoMo7rr6D0T25qk1k6TZ9iLI4sfCghc9hzSZQpY21SZV_Pdm6epRw5AE8sy85CHkEmgOFOTNLg_YGVvnjALklKViR2QOtJIZl1wc7--lyKqCwYychbCjlIqKyVMyY8ALwWE1J7DxEQdtout9WNYYPxH90vc-cxZ9dEa3y7chPaa9j-h8OCcnjW4DXhzOBXl9uH9ZP2Xb58fN-m6bGV7xmK2oKaTRvLGlEboWWnOubZFW2ViQ1sjKStSlqWstAQtdcyYpRbAJEgB8Qa6nuSn4fcQQVeeCwbbVHvsxqAoACiFK-T9JuZQgZZlIMZFm6EMYsFHpb50evhRQtbeqdmqyqvZWFWWpWGq7OgSMdYf2t-lHYwJuJwCTkA-HgwrGoTdo3YAmKtu7vxO-AXynigo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>903661668</pqid></control><display><type>article</type><title>Interactions between non-identical prion proteins</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Gonzalez Nelson, Aaron C. ; Ross, Eric D.</creator><creatorcontrib>Gonzalez Nelson, Aaron C. ; Ross, Eric D.</creatorcontrib><description>Prion formation involves the conversion of soluble proteins into an infectious amyloid form. This process is highly specific, with prion aggregates templating the conversion of identical proteins. However, in some cases non-identical prion proteins can interact to promote or inhibit prion formation or propagation. These interactions affect both the efficiency with which prion diseases are transmitted across species and the normal physiology of yeast prion formation and propagation. Here we examine two types of heterologous prion interactions: interactions between related proteins from different species (the species barrier) and interactions between unrelated prion proteins within a single species. Interestingly, although very subtle changes in protein sequence can significantly reduce or eliminate cross-species prion transmission, in Saccharomyces cerevisiae completely unrelated prion proteins can interact to affect prion formation and propagation.</description><identifier>ISSN: 1084-9521</identifier><identifier>EISSN: 1096-3634</identifier><identifier>DOI: 10.1016/j.semcdb.2011.02.022</identifier><identifier>PMID: 21354317</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amyloid ; Amyloid - metabolism ; Glutathione Peroxidase - chemistry ; Glutathione Peroxidase - metabolism ; Models, Molecular ; Plasmids - genetics ; Prion ; Prions - chemistry ; Prions - metabolism ; Protein Structure, Quaternary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Species barrier ; Species Specificity ; Yeast</subject><ispartof>Seminars in cell &amp; developmental biology, 2011-07, Vol.22 (5), p.437-443</ispartof><rights>2011 Elsevier Ltd</rights><rights>Copyright © 2011 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-70c56ca3fd8c4ab4aa33ad55558fd16dc69d6ea8cbba61e5ab32600e1dd554113</citedby><cites>FETCH-LOGICAL-c393t-70c56ca3fd8c4ab4aa33ad55558fd16dc69d6ea8cbba61e5ab32600e1dd554113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.semcdb.2011.02.022$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21354317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gonzalez Nelson, Aaron C.</creatorcontrib><creatorcontrib>Ross, Eric D.</creatorcontrib><title>Interactions between non-identical prion proteins</title><title>Seminars in cell &amp; developmental biology</title><addtitle>Semin Cell Dev Biol</addtitle><description>Prion formation involves the conversion of soluble proteins into an infectious amyloid form. This process is highly specific, with prion aggregates templating the conversion of identical proteins. However, in some cases non-identical prion proteins can interact to promote or inhibit prion formation or propagation. These interactions affect both the efficiency with which prion diseases are transmitted across species and the normal physiology of yeast prion formation and propagation. Here we examine two types of heterologous prion interactions: interactions between related proteins from different species (the species barrier) and interactions between unrelated prion proteins within a single species. Interestingly, although very subtle changes in protein sequence can significantly reduce or eliminate cross-species prion transmission, in Saccharomyces cerevisiae completely unrelated prion proteins can interact to affect prion formation and propagation.</description><subject>Amyloid</subject><subject>Amyloid - metabolism</subject><subject>Glutathione Peroxidase - chemistry</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Models, Molecular</subject><subject>Plasmids - genetics</subject><subject>Prion</subject><subject>Prions - chemistry</subject><subject>Prions - metabolism</subject><subject>Protein Structure, Quaternary</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Species barrier</subject><subject>Species Specificity</subject><subject>Yeast</subject><issn>1084-9521</issn><issn>1096-3634</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMo7rr6D0T25qk1k6TZ9iLI4sfCghc9hzSZQpY21SZV_Pdm6epRw5AE8sy85CHkEmgOFOTNLg_YGVvnjALklKViR2QOtJIZl1wc7--lyKqCwYychbCjlIqKyVMyY8ALwWE1J7DxEQdtout9WNYYPxH90vc-cxZ9dEa3y7chPaa9j-h8OCcnjW4DXhzOBXl9uH9ZP2Xb58fN-m6bGV7xmK2oKaTRvLGlEboWWnOubZFW2ViQ1sjKStSlqWstAQtdcyYpRbAJEgB8Qa6nuSn4fcQQVeeCwbbVHvsxqAoACiFK-T9JuZQgZZlIMZFm6EMYsFHpb50evhRQtbeqdmqyqvZWFWWpWGq7OgSMdYf2t-lHYwJuJwCTkA-HgwrGoTdo3YAmKtu7vxO-AXynigo</recordid><startdate>20110701</startdate><enddate>20110701</enddate><creator>Gonzalez Nelson, Aaron C.</creator><creator>Ross, Eric D.</creator><general>Elsevier Ltd</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><scope>7TK</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20110701</creationdate><title>Interactions between non-identical prion proteins</title><author>Gonzalez Nelson, Aaron C. ; Ross, Eric D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-70c56ca3fd8c4ab4aa33ad55558fd16dc69d6ea8cbba61e5ab32600e1dd554113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amyloid</topic><topic>Amyloid - metabolism</topic><topic>Glutathione Peroxidase - chemistry</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Models, Molecular</topic><topic>Plasmids - genetics</topic><topic>Prion</topic><topic>Prions - chemistry</topic><topic>Prions - metabolism</topic><topic>Protein Structure, Quaternary</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - chemistry</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Species barrier</topic><topic>Species Specificity</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gonzalez Nelson, Aaron C.</creatorcontrib><creatorcontrib>Ross, Eric D.</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><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Seminars in cell &amp; developmental biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gonzalez Nelson, Aaron C.</au><au>Ross, Eric D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between non-identical prion proteins</atitle><jtitle>Seminars in cell &amp; developmental biology</jtitle><addtitle>Semin Cell Dev Biol</addtitle><date>2011-07-01</date><risdate>2011</risdate><volume>22</volume><issue>5</issue><spage>437</spage><epage>443</epage><pages>437-443</pages><issn>1084-9521</issn><eissn>1096-3634</eissn><abstract>Prion formation involves the conversion of soluble proteins into an infectious amyloid form. This process is highly specific, with prion aggregates templating the conversion of identical proteins. However, in some cases non-identical prion proteins can interact to promote or inhibit prion formation or propagation. These interactions affect both the efficiency with which prion diseases are transmitted across species and the normal physiology of yeast prion formation and propagation. Here we examine two types of heterologous prion interactions: interactions between related proteins from different species (the species barrier) and interactions between unrelated prion proteins within a single species. Interestingly, although very subtle changes in protein sequence can significantly reduce or eliminate cross-species prion transmission, in Saccharomyces cerevisiae completely unrelated prion proteins can interact to affect prion formation and propagation.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>21354317</pmid><doi>10.1016/j.semcdb.2011.02.022</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1084-9521
ispartof Seminars in cell & developmental biology, 2011-07, Vol.22 (5), p.437-443
issn 1084-9521
1096-3634
language eng
recordid cdi_proquest_miscellaneous_911154486
source MEDLINE; Access via ScienceDirect (Elsevier)
subjects Amyloid
Amyloid - metabolism
Glutathione Peroxidase - chemistry
Glutathione Peroxidase - metabolism
Models, Molecular
Plasmids - genetics
Prion
Prions - chemistry
Prions - metabolism
Protein Structure, Quaternary
Saccharomyces cerevisiae
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Species barrier
Species Specificity
Yeast
title Interactions between non-identical prion proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T08%3A37%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interactions%20between%20non-identical%20prion%20proteins&rft.jtitle=Seminars%20in%20cell%20&%20developmental%20biology&rft.au=Gonzalez%20Nelson,%20Aaron%20C.&rft.date=2011-07-01&rft.volume=22&rft.issue=5&rft.spage=437&rft.epage=443&rft.pages=437-443&rft.issn=1084-9521&rft.eissn=1096-3634&rft_id=info:doi/10.1016/j.semcdb.2011.02.022&rft_dat=%3Cproquest_cross%3E911154486%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=903661668&rft_id=info:pmid/21354317&rft_els_id=S1084952111000358&rfr_iscdi=true