Results

RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/16642217http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16642217http://www.w3.org/2000/01/rdf-schema#comment"

Background

To investigate the dynamics of amyloid fiber formation of yeast (Saccharomyces cerevisiae) prion protein Sup35NM under the native condition to provide materials and clues for the elucidation of amyloid fiber formation.

Methods

The Sup35NM gene was cloned and expressed in E. coli. The recombinant Sup35NM protein was purified under denaturing conditions through Nickel-Sepharose chromatography. Aliquots were removed at designated time points for transmission electron microscopy (TEM), circular dichroism (CD) spectra, protease K resistance assay, as well as thioflavin T (ThT) binding assay.

Results

The Sup35NM expressed and purified under denaturing conditions. The morphological alteration of the Sup35NM in PBS (pH7.4) during the protein aggregation and amyloid fiber formation was visualized by TEM. The CD assay showed that the course of amyloid fiber formation underwent a conformational shift from alpha-helix to beta-sheet. The fibers had higher capacity of resistance to protease K digestion compared to the monomers. ThT fluorescence assay displayed a rapid growth phase before reaching a final equilibrium phase during the fiber formation, and the higher concentration of Sup35NM could greatly accelerate the fiber formation in vitro.

Conclusion

Yeast prion protein Sup35NM forms amyloid readily under native conditions in vitro. The dynamics of Sup35NM amyloid formation may provide supporting evidences for the nucleating polymerization models of amyloid fiber formation."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Liu Y.X."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Hong T."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Zhao W.M."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Wang J.W."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Wei H.Y."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Yu X.P."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/author"Qu J.G."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/name"Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi"xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/pages"39-42"xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/title"[Dynamics of in vitro amyloid fiber formation of yeast prion protein Sup35NM]."xsd:string
http://purl.uniprot.org/citations/16642217http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/16642217http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16642217
http://purl.uniprot.org/citations/16642217http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16642217
http://purl.uniprot.org/uniprot/#_P05453-mappedCitation-16642217http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16642217
http://purl.uniprot.org/uniprot/P05453http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16642217