Analyzing the Birth and Propagation of Two Distinct Prions, [PSI+] and [Het-s]y, in Yeast
Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin
protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid
formation. Other prions, eg, mammalian PrP and the [Het-s] prion of Podospora anserina,
although still able to form infectious amyloid aggregates, do not have QN-rich regions.
Furthermore,[Het-s] and yeast prions appear to differ dramatically in their amyloid
conformation. Despite these differences, a fusion of the Het-s prion domain to GFP (Het …
protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid
formation. Other prions, eg, mammalian PrP and the [Het-s] prion of Podospora anserina,
although still able to form infectious amyloid aggregates, do not have QN-rich regions.
Furthermore,[Het-s] and yeast prions appear to differ dramatically in their amyloid
conformation. Despite these differences, a fusion of the Het-s prion domain to GFP (Het …
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