Abstract：
:Formation of filaments by the Ure2 protein constitutes the molecular mechanism of the [URE3] prion in yeast. According to the "amyloid backbone" model, the N-terminal asparagine-rich domains of Ure2p polymerize to form an amyloid core fibril that is surrounded by C-terminal domains in their native conformation. Protease resistance and Congo Red binding as well as beta-sheet content detected by spectroscopy-all markers for amyloid-have supported this model, as has the close resemblance between 40 A N-domain fibrils and the fibrillar core of intact Ure2p filaments visualized by cryo-electron microscopy and scanning transmission electron microscopy. Here, we present electron diffraction and X-ray diffraction data from filaments of Ure2p, of N-domains alone, of fragments thereof, and of an N-domain-containing fusion protein that demonstrate in each case the 4.7A reflection that is typical for cross-beta structure and highly indicative of amyloid. This reflection was observed for specimens prepared by air-drying with and without sucrose embedding. To confirm that the corresponding structure is not an artifact of air-drying, the reflection was also demonstrated for specimens preserved in vitreous ice. Local area electron diffraction and X-ray diffraction from partially aligned specimens showed that the 4.7A reflection is meridional and therefore the underlying structure is cross-beta.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Baxa U,Cheng N,Winkler DC,Chiu TK,Davies DR,Sharma D,Inouye H,Kirschner DA,Wickner RB,Steven ACdoi
10.1016/j.jsb.2005.02.007keywords:
subject
Has Abstractpub_date
2005-05-01 00:00:00pages
170-9issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(05)00049-3journal_volume
150pub_type
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