Cellular toxicity of yeast prion protein Rnq1 can be modulated by N-terminal wild type huntingtin
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- 作者：Ratnika Sethi ; Vishal Patel ; Aliabbas A. Saleh ; Ipsita Roy ; ipsita@niper.ac.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：Chaperone ; Huntingtin ; Protein aggregation ; Prions
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 January 2016
- 年：2016
- 卷：590
- 期：Complete
- 页码：82-89
- 全文大小：1124 K
文摘
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Yeast prion protein Rnq1p forms intracellular amyloid aggregates.
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Presence of N-terminal wild-type huntingtin fragment solubilizes Rnq1p.
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Increased solubility reduces oxidative stress and increases cell survival.
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Overexpression of Rnq1p sequesters N-terminal wild-type huntingtin fragment.
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Even here, effect of the polyglutamine-rich protein on cellular phenotype is obvious.