Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures
نویسندگان
چکیده
منابع مشابه
Yeast prions: Inheritance by seeded protein polymerization?
The discovery that RNA enzymes — ribozymes — can fulfill a function previously thought to be the exclusive province of proteins has had far-reaching implications. It has recently become apparent that certain proteins may have the ability to transmit information and to self-replicate, functions normally associated with nucleic acids. The first self-replicating entity proposed to be ‘protein-only...
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The [PSI(+)] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly ch...
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β-amyloid hypothesis is the predominant hypothesis in the study of pathogenesis of Alzheimer's disease. This hypothesis claims that aggregation and neurotoxic effects of amyloid β (Aβ) is the common pathway in a variety of etiological factors for Alzheimer's disease. Aβ peptide derives from amyloid precursor protein (APP). β-sheet breaker peptides can directly prevent and reverse protein misfol...
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Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements. Fungal prions correspond in most cases to fibrillary β-sheet-rich protein aggregates termed amyloids. Fungal prion models and, in particular, yeast prions were ins...
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Protein amyloid oligomers have been strongly linked to amyloid diseases and can be intermediates to amyloid fibers. β-Sheets have been identified in amyloid oligomers. However, because of their transient and highly polymorphic properties, the details of their self-association remain elusive. Here we explore oligomer structure using a model system: macrocyclic peptides. Key amyloidogenic sequenc...
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ژورنال
عنوان ژورنال: BioEssays
سال: 2008
ISSN: 0265-9247,1521-1878
DOI: 10.1002/bies.20821