Single-stranded DNA aptamers interacting with fibers formed by the Sup35 protein of Saccharomyces cerevisiae were obtained by the SELEX procedure. Specificity of interaction with Sup35p is investigated for 10 from total of 40 selected aptamers. It is shown that 9 aptamers bind to fibrillar Sup35p and not to monomeric form of the protein.
View Article and Find Full Text PDFAmyloids are fibrous protein aggregates which arise due to polymerization of proteins accompanied by their conformational rearrangement and formation of a specific "cross-beta" structure. The interest to amyloids is caused by their relation to a vast group of human and animal diseases called amyloidoses. Some of these diseases caused by prions, a specific type of amyloids, are transmissible.
View Article and Find Full Text PDFMore than 20 human diseases are related to protein misfolding which causes formation of amyloids, fibrillar aggregates of normally soluble proteins. Such diseases are called amyloid diseases or amyloidoses. Of them only prion diseases are transmissible.
View Article and Find Full Text PDFThe cell's failure to refold or break down abnormal polypeptides often leads to their aggregation, which could cause toxicity and various pathologies. Here we investigated cellular factors involved in protein aggregation in yeast and mammalian cells using model polypeptides containing polyglutamine domains. In yeast, a number of mutations affecting the complex responsible for formation of the endocytic vesicle reduced the aggregation.
View Article and Find Full Text PDFThe Mcd4 protein of Saccharomyces cerevisiae is probably involved in addition of the phosphoethanolamine moiety to the first mannose residue of the glycosylphosphatidylinositol precursor(s). However, significance of this modification is unclear. Besides, functions of the MCD4 gene also is not completely clear, since mutations in this gene may have pleiotropic manifestations, which are not obviously related to the glycosylphosphatidylinositol biosynthesis.
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