scholarly journals Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein

2021 ◽  
Author(s):  
Arnab Bandyopadhyay ◽  
Achinta Sannigrahi ◽  
Krishnananda Chattopadhyay
Keyword(s):  
Prion Protein ◽  
Membrane Composition ◽  
Yeast Prion ◽  
Protein Ratio ◽  
Kinetics Of

This study provides a mechanistic description of how the membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein.

scholarly journals Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein

2020 ◽  
Author(s):  
Arnab Bandyopadhyay ◽  
Achinta Sannigrahi ◽  
Krishnananda Chattopadhyay
Keyword(s):  
Prion Protein ◽  
Single Molecule ◽  
Correlation Spectroscopy ◽  
Aggregation Kinetics ◽  
Membrane Composition ◽  
Yeast Prion ◽  
Lipid Concentration ◽  
Protein Ratio ◽  
Induced Aggregation ◽  
Kinetics Of

AbstractUnderstanding of prion aggregation in membrane environment may help to ameliorate neurodegenerative complications caused by the amyloid forms of prions. Here, we investigated the membrane binding induced aggregation of yeast prion protein Sup35. Using the combination of fluorescence correlation spectroscopy (FCS) at single molecule resolution and other biophysical studies, we establish that lipid composition and lipid/protein ratio are key modulators of the aggregation kinetics of Sup35. In the presence of zwitterionic membrane, Sup35 exhibited a novel biphasic aggregation kinetics at lipid/protein ratio ranging between 20:1 and 70:1 (termed here as the Optimum Lipid Concentration, OLC). In ratios below (Low Lipid Concentration, LLC) and above (ELC, Excess Lipid Concentration) that range, the aggregation was found to be monophasic. In contrast, in the presence of negatively charged membrane, we did not observe any bi-phasic aggregation kinetics in the entire range of protein to lipid ratios. The toxicity of the aggregates formed within OLC range was found to be greater. Our results provide a mechanistic description of the role that membrane-concentration/composition-modulated-aggregation may play in neurodegenerative diseases.

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 Hsp104 Overexpression Cures Saccharomyces cerevisiae [ PSI + ] by Causing Dissolution of the Prion Seeds

2014 ◽  
Vol 13 (5) ◽  
pp. 635-647 ◽  
Author(s):  
Yang-Nim Park ◽  
Xiaohong Zhao ◽  
Yang-In Yim ◽  
Horia Todor ◽  
Robyn Ellerbrock ◽  
...  
Keyword(s):  
Molecular Chaperone ◽  
Fluorescent Protein ◽  
Yeast Cells ◽  
Yeast Prion ◽  
Yeast Prions ◽  
Daughter Cells ◽  
Amyloid Aggregates ◽  
Mother And Daughter ◽  
Green Fluorescent ◽  
Kinetics Of

ABSTRACT The [ PSI + ] yeast prion is formed when Sup35 misfolds into amyloid aggregates. [ PSI + ], like other yeast prions, is dependent on the molecular chaperone Hsp104, which severs the prion seeds so that they pass on as the yeast cells divide. Surprisingly, however, overexpression of Hsp104 also cures [ PSI + ]. Several models have been proposed to explain this effect: inhibition of severing, asymmetric segregation of the seeds between mother and daughter cells, and dissolution of the prion seeds. First, we found that neither the kinetics of curing nor the heterogeneity in the distribution of the green fluorescent protein (GFP)-labeled Sup35 foci in partially cured yeast cells is compatible with Hsp104 overexpression curing [ PSI + ] by inhibiting severing. Second, we ruled out the asymmetric segregation model by showing that the extent of curing was essentially the same in mother and daughter cells and that the fluorescent foci did not distribute asymmetrically, but rather, there was marked loss of foci in both mother and daughter cells. These results suggest that Hsp104 overexpression cures [ PSI + ] by dissolution of the prion seeds in a two-step process. First, trimming of the prion seeds by Hsp104 reduces their size, and second, their amyloid core is eliminated, most likely by proteolysis.

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

Real-time kinetics of discontinuous and highly conformational metal-ion binding sites of prion protein

2007 ◽  
Vol 12 (5) ◽  
pp. 711-720 ◽  
Author(s):  
Carina Treiber ◽  
Andrew R. Thompsett ◽  
Rüdiger Pipkorn ◽  
David R. Brown ◽  
Gerd Multhaup
Keyword(s):  
Real Time ◽  
Prion Protein ◽  
Binding Sites ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ion Binding Sites ◽  
Metal Ion Binding Sites ◽  
Kinetics Of

scholarly journals The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p

2001 ◽  
Vol 98 (4) ◽  
pp. 1459-1464 ◽  
Author(s):  
T. C. Umland ◽  
K. L. Taylor ◽  
S. Rhee ◽  
R. B. Wickner ◽  
D. R. Davies
Keyword(s):  
Crystal Structure ◽  
Prion Protein ◽  
Nitrogen Regulation ◽  
Yeast Prion

scholarly journals Effects of Electrostatics on Interactions of Short Peptide from Yeast Prion Protein Sup35

2011 ◽  
Vol 100 (3) ◽  
pp. 162a
Author(s):  
Alexander M. Portillo ◽  
Alexey V. Krasnoslobodtsev ◽  
Yuri L. Lyubchenko
Keyword(s):  
Prion Protein ◽  
Yeast Prion ◽  
Short Peptide

Cellular toxicity of yeast prion protein Rnq1 can be modulated by N-terminal wild type huntingtin

2016 ◽  
Vol 590 ◽  
pp. 82-89
Author(s):  
Ratnika Sethi ◽  
Vishal Patel ◽  
Aliabbas A. Saleh ◽  
Ipsita Roy
Keyword(s):  
Prion Protein ◽  
Yeast Prion ◽  
Wild Type ◽  
Cellular Toxicity
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