scholarly journals The Hofmeister effect on amyloid formation using yeast prion protein

2009 ◽  
Vol 19 (1) ◽  
pp. 47-56 ◽  
Author(s):  
Victor Yeh ◽  
James M. Broering ◽  
Andrey Romanyuk ◽  
Buxin Chen ◽  
Yury O. Chernoff ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Formation ◽  
Yeast Prion ◽  
Hofmeister Effect

Amyloid formation characteristics of GNNQQNY from yeast prion protein Sup35 and its seeding with heterogeneous polypeptides

2017 ◽  
Vol 149 ◽  
pp. 72-79 ◽  
Author(s):  
Mamoru Haratake ◽  
Tohru Takiguchi ◽  
Naho Masuda ◽  
Sakura Yoshida ◽  
Takeshi Fuchigami ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Formation ◽  
Yeast Prion

The yeast prion protein Ure2: insights into the mechanism of amyloid formation

2011 ◽  
Vol 39 (5) ◽  
pp. 1359-1364 ◽  
Author(s):  
Li-Jun Chen ◽  
Elizabeth B. Sawyer ◽  
Sarah Perrett
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Conformational Change ◽  
Nitrogen Metabolism ◽  
Prion Protein ◽  
Molecular Chaperones ◽  
Fibril Formation ◽  
Regulatory Function ◽  
Amyloid Formation ◽  
Yeast Prion

Ure2, a regulator of nitrogen metabolism, is the protein determinant of the [URE3] prion state in Saccharomyces cerevisiae. Upon conversion into the prion form, Ure2 undergoes a heritable conformational change to an amyloid-like aggregated state and loses its regulatory function. A number of molecular chaperones have been found to affect the prion properties of Ure2. The studies carried out in our laboratory have been aimed at elucidating the structure of Ure2 fibrils, the mechanism of amyloid formation and the effect of chaperones on the fibril formation of Ure2.

scholarly journals Compositional Determinants of Prion Formation in Yeast

2009 ◽  
Vol 30 (1) ◽  
pp. 319-332 ◽  
Author(s):  
James A. Toombs ◽  
Blake R. McCarty ◽  
Eric D. Ross
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Amyloid Formation ◽  
Yeast Prion ◽  
Hydrophobic Residues ◽  
Predictive Methods ◽  
Infectious Proteins ◽  
Β Sheet ◽  
Eukaryotic Genomes

ABSTRACT Numerous prions (infectious proteins) have been identified in yeast that result from the conversion of soluble proteins into β-sheet-rich amyloid-like protein aggregates. Yeast prion formation is driven primarily by amino acid composition. However, yeast prion domains are generally lacking in the bulky hydrophobic residues most strongly associated with amyloid formation and are instead enriched in glutamines and asparagines. Glutamine/asparagine-rich domains are thought to be involved in both disease-related and beneficial amyloid formation. These domains are overrepresented in eukaryotic genomes, but predictive methods have not yet been developed to efficiently distinguish between prion and nonprion glutamine/asparagine-rich domains. We have developed a novel in vivo assay to quantitatively assess how composition affects prion formation. Using our results, we have defined the compositional features that promote prion formation, allowing us to accurately distinguish between glutamine/asparagine-rich domains that can form prion-like aggregates and those that cannot. Additionally, our results explain why traditional amyloid prediction algorithms fail to accurately predict amyloid formation by the glutamine/asparagine-rich yeast prion domains.

scholarly journals The Prion Protein Octarepeat Domain Forms Transient β-sheet Structures Upon Residue-Specific Cu(II) and Zn(II) Binding

2021 ◽  
Author(s):  
Maciej Gielnik ◽  
Aneta Szymanska ◽  
Xiaolin Dong ◽  
Jyri Jarvet ◽  
Zeljko M. Svedruzic ◽  
...  
Keyword(s):  
Metal Ions ◽  
Prion Protein ◽  
Metal Binding ◽  
Cd Spectroscopy ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Amyloid Formation ◽  
Spectroscopy Data ◽  
Spongiform Encephalopathies ◽  
Β Sheet

Misfolding of the cellular prion protein (PrPC) is associated with the development of fatal neurodegenerative diseases called transmissible spongiform encephalopathies (TSEs). Metal ions appear to play a crucial role in the protein misfolding, and metal imbalance may be part of TSE pathologies. PrPC is a combined Cu(II) and Zn(II) metal binding protein, where the main metal binding site is located in the octarepeat (OR) region. Here, we used biophysical methods to characterize Cu(II) and Zn(II) binding to the isolated OR region. Circular dichroism (CD) spectroscopy data suggest that the OR domain binds up to four Cu(II) ions or two Zn(II) ions. Upon metal binding, the OR region seems to adopt a transient antiparallel β-sheet hairpin structure. Fluorescence spectroscopy data indicates that under neutral conditions, the OR region can bind both Cu(II) and Zn(II) ions, whereas under acidic conditions it binds only Cu(II) ions. Molecular dynamics simulations suggest that binding of both metal ions to the OR region results in formation of β-hairpin structures. As formation of β-sheet structures is a first step towards amyloid formation, we propose that high concentrations of either Cu(II) or Zn(II) ions may have a pro-amyloid effect in TSEs.

scholarly journals Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils

2007 ◽  
Vol 282 (16) ◽  
pp. 11931-11940 ◽  
Author(s):  
Hui-Yong Lian ◽  
Hong Zhang ◽  
Zai-Rong Zhang ◽  
Harriët M. Loovers ◽  
Gary W. Jones ◽  
...  
Keyword(s):  
Prion Protein ◽  
Yeast Prion ◽  
Native State

scholarly journals Parallel β-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10−39 of the Yeast Prion Protein Ure2p

Biochemistry ◽  
2005 ◽  
Vol 44 (31) ◽  
pp. 10669-10680 ◽  
Author(s):  
Jerry C. C. Chan ◽  
Nathan A. Oyler ◽  
Wai-Ming Yau ◽  
Robert Tycko
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Yeast Prion ◽  
Β Sheets
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