有哪些信誉好的足球投注网站amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeastamyloid-mediated封存基本蛋白质有助于突变杭丁顿蛋白在酵母毒性.pdfVIP
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amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeastamyloid-mediated封存基本蛋白质有助于突变杭丁顿蛋白在酵母毒性
Amyloid-Mediated Sequestration of Essential Proteins
Contributes to Mutant Huntingtin Toxicity in Yeast
. .
Natalia V. Kochneva-Pervukhova , Alexander I. Alexandrov , Michael D. Ter-Avanesyan*
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia
Abstract
Background: Polyglutamine expansion is responsible for several neurodegenerative disorders, among which Huntington
disease is the most well-known. Studies in the yeast model demonstrated that both aggregation and toxicity of a huntingtin
(htt) protein with an expanded polyglutamine region strictly depend on the presence of the prion form of Rnq1 protein
([PIN+]), which has a glutamine/asparagine-rich domain.
+
Principal Findings: Here, we showed that aggregation and toxicity of mutant htt depended on [PIN ] only quantitatively:
the presence of [PIN+ +
] elevated the toxicity and the levels of htt detergent-insoluble polymers. In cells lacking [PIN ], toxicity
of mutant htt was due to the polymerization and inactivation of the essential glutamine/asparagine-rich Sup35 protein and
related inactivation of another essential protein, Sup45, most probably via its sequestration into Sup35 aggregates.
However, inhibition of growth of [PIN+] cells depended on Sup35/Sup45 depletion only partially, suggesting that there are
other sources of mutant htt toxicity in yeast.
Conclusions: The obtained data suggest that induced polymerization of essential glutamine/asparagine-rich protein
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