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Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1

Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1

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ERHARDT, Marc, Renee D. WEGRZYN, Elke DEUERLING, 2010. Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1. In: PLoS ONE. 5(3), e9929. eISSN 1932-6203. Available under: doi: 10.1371/journal.pone.0009929

@article{Erhardt2010Extra-12512, title={Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1}, year={2010}, doi={10.1371/journal.pone.0009929}, number={3}, volume={5}, journal={PLoS ONE}, author={Erhardt, Marc and Wegrzyn, Renee D. and Deuerling, Elke}, note={Article Number: e9929} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/12512"> <dcterms:bibliographicCitation>First publ. in: PLoS ONE 5 (2010), 3, e9929</dcterms:bibliographicCitation> <dc:creator>Deuerling, Elke</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-06-20T07:52:27Z</dcterms:available> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Deuerling, Elke</dc:contributor> <dc:contributor>Wegrzyn, Renee D.</dc:contributor> <dc:language>eng</dc:language> <dcterms:title>Extra N-Terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1</dcterms:title> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/12512/1/erhardt.pdf"/> <dc:creator>Erhardt, Marc</dc:creator> <dcterms:issued>2010</dcterms:issued> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/12512/1/erhardt.pdf"/> <dc:rights>deposit-license</dc:rights> <dc:creator>Wegrzyn, Renee D.</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-06-20T07:52:27Z</dc:date> <dc:contributor>Erhardt, Marc</dc:contributor> <dcterms:abstract xml:lang="eng">The metacaspase Mca1 from Saccharomyces cerevisiae displays a Q/N-rich region at its N-terminus reminiscent of yeast prion proteins. In this study, we show that the ability of Mca1 to form insoluble aggregates is modulated by a peptide stretch preceding its putative prion-forming domain. Based on its genomic locus, three potential translational start sites of Mca1 can give rise to two slightly different long Mca1 proteins or a short version, Mca1451/453 and Mca1432, respectively, although under normal physiological conditions Mca1432 is the predominant form expressed. All Mca1 variants exhibit the Q/N-rich regions, while only the long variants Mca1451/453 share an extra stretch of 19 amino acids at their N-terminal end. Strikingly, only long versions of Mca1 but not Mca1432 revealed pronounced aggregation in vivo and displayed prion-like properties when fused to the C-terminal domain of Sup35 suggesting that the N-terminal peptide element promotes the conformational switch of Mca1 protein into an insoluble state. Transfer of the 19 N-terminal amino acid stretch of Mca1451 to the N-terminus of firefly luciferase resulted in increased aggregation of luciferase, suggesting a protein destabilizing function of the peptide element. We conclude that the aggregation propensity of the potential yeast prion protein Mca1 in vivo is strongly accelerated by a short peptide segment preceding its Q/N-rich region and we speculate that such a conformational switch might occur in vivo via the usage of alternative translational start sites.</dcterms:abstract> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/12512"/> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> </rdf:Description> </rdf:RDF>

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