Linked Life Data

12917441

Source:http://linkedlifedata.com/resource/pubmed/id/12917441

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2003-10-27
pubmed:abstractText
The [URE3] prion is an inactive, self-propagating, filamentous form of the Ure2 protein, a regulator of nitrogen catabolism in yeast. The N-terminal "prion" domain of Ure2p determines its in vivo prion properties and in vitro amyloid-forming ability. Here we determined the overall structures of Ure2p filaments and related polymers of the prion domain fused to other globular proteins. Protease digestion of 25-nm diameter Ure2p filaments trimmed them to 4-nm filaments, which mass spectrometry showed to be composed of prion domain fragments, primarily residues approximately 1-70. Fusion protein filaments with diameters of 14-25 nm were also reduced to 4-nm filaments by proteolysis. The prion domain transforms from the most to the least protease-sensitive part upon filament formation in each case, implying that it undergoes a conformational change. Intact filaments imaged by cryo-electron microscopy or after vanadate staining by scanning transmission electron microscopy (STEM) revealed a central 4-nm core with attached globular appendages. STEM mass per unit length measurements of unstained filaments yielded 1 monomer per 0.45 nm in each case. These observations strongly support a unifying model whereby subunits in Ure2p filaments, as well as in fusion protein filaments, are connected by interactions between their prion domains, which form a 4-nm amyloid filament backbone, surrounded by the corresponding C-terminal moieties.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43717-27
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12917441-Blotting, Western, pubmed-meshheading:12917441-Chromatography, Liquid, pubmed-meshheading:12917441-Cloning, Molecular, pubmed-meshheading:12917441-Cryoelectron Microscopy, pubmed-meshheading:12917441-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12917441-Endopeptidase K, pubmed-meshheading:12917441-Glutathione Peroxidase, pubmed-meshheading:12917441-Mass Spectrometry, pubmed-meshheading:12917441-Microscopy, Electron, pubmed-meshheading:12917441-Microscopy, Electron, Scanning Transmission, pubmed-meshheading:12917441-Polymers, pubmed-meshheading:12917441-Prions, pubmed-meshheading:12917441-Protein Conformation, pubmed-meshheading:12917441-Protein Structure, Tertiary, pubmed-meshheading:12917441-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12917441-Time Factors, pubmed-meshheading:12917441-Trypsin
pubmed:year
2003
pubmed:articleTitle
Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber.
pubmed:affiliation
Laboratories of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, and Biochemistry and Genetics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article