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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1997-1-23
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pubmed:abstractText |
The unusual genetic behaviour of two yeast extrachromosomal elements [PSI] and [URE3] is entirely consistent with a prion-like mechanism of inheritance involving an autocatalytic alteration in the conformation of a normal cellular protein. In the case of both yeast determinants the identity of the underlying cellular prion protein is known. The discovery that the molecular chaperone Hsp104 is essential for the establishment and maintenance of the [PSI] determinant provides an explanation for several aspects of the puzzling genetic behaviour of these determinants. What remains to be explained is whether these determinants represent 'disease states' of yeast or represent the first examples of a unique mechanism for producing a heritable change in phenotype without an underlying change in genotype.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HsP104 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Termination Factors,
http://linkedlifedata.com/resource/pubmed/chemical/PrPC Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PrPSc Proteins,
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/URE2 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0168-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
467-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8973157-Fungal Proteins,
pubmed-meshheading:8973157-Gene Expression Regulation, Fungal,
pubmed-meshheading:8973157-Glutathione Peroxidase,
pubmed-meshheading:8973157-Heat-Shock Proteins,
pubmed-meshheading:8973157-Models, Biological,
pubmed-meshheading:8973157-Peptide Termination Factors,
pubmed-meshheading:8973157-PrPC Proteins,
pubmed-meshheading:8973157-PrPSc Proteins,
pubmed-meshheading:8973157-Prions,
pubmed-meshheading:8973157-Protein Conformation,
pubmed-meshheading:8973157-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8973157-Yeasts
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pubmed:year |
1996
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pubmed:articleTitle |
Maintenance and inheritance of yeast prions.
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pubmed:affiliation |
Research School of Biosciences, University of Kent, Canterbury, UK. m.f.tuite@ukc.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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