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...
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Veröffentlicht in: | Seminars in cell & developmental biology 2011-07, Vol.22 (5), p.437-443 |
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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 |
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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 & 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 & 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. 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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 |
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