Source:http://linkedlifedata.com/resource/pubmed/id/19160487
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
2009-1-22
|
pubmed:abstractText |
Prion proteins are found in mammals and yeast, and can transmit diseases and encode heritable phenotypic traits. In Saccharomyces cerevisiae, eRF3, Rnq1, Ure2 and Swil are functional proteins with a soluble conformation that can switch to a non-functional, amyloid conformation denoted as [PSI+], [PIN+], [URE3] and [SWI+], respectively. The prion [PSI+] corresponds to an aggregated conformation of the translational release factor eRF3, which suppresses nonsense codons. [PSI+] modifies cellular fitness and induces several phenotypes according to the genetic background. An elegant series of studies has demonstrated that several [PSI+]-induced phenotypes occur as a consequence of decreased translational termination efficiency. However, the genes whose expression levels are controlled by [PSI+] remain largely unknown. Here, we show that [PSI+] enhances expression of antizyme, a negative regulator of cellular polyamines, by modulating the +1 frameshifting required for its expression. Our study also demonstrates that [PSI+] greatly affects cellular polyamines in yeast. We show that modification of the cellular content of polyamines by the prion accounts for half of the [PSI+]-induced phenotypes. Antizyme is the first protein to be described for which expression of its functional form is stimulated by [PSI+].
|
pubmed:commentsCorrections | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Termination Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Polyamines,
http://linkedlifedata.com/resource/pubmed/chemical/Prions,
http://linkedlifedata.com/resource/pubmed/chemical/SUP35 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/peptide-chain-release factor 3
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
1465-7392
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
10
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1069-75
|
pubmed:dateRevised |
2009-7-3
|
pubmed:meshHeading |
pubmed-meshheading:19160487-Epigenesis, Genetic,
pubmed-meshheading:19160487-Intracellular Space,
pubmed-meshheading:19160487-Models, Biological,
pubmed-meshheading:19160487-Peptide Termination Factors,
pubmed-meshheading:19160487-Phenotype,
pubmed-meshheading:19160487-Polyamines,
pubmed-meshheading:19160487-Prions,
pubmed-meshheading:19160487-Saccharomyces cerevisiae,
pubmed-meshheading:19160487-Saccharomyces cerevisiae Proteins
|
pubmed:year |
2008
|
pubmed:articleTitle |
Epigenetic control of polyamines by the prion [PSI+].
|
pubmed:affiliation |
IGM, CNRS, UMR 8621, Orsay, 91405 France. olivier.namy@igmors.u-psud.fr
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|