Rnq1 protein protects [PSI+] prion from effect of the PNM mutation


如何引用文章

全文:

开放存取 开放存取
受限制的访问 ##reader.subscriptionAccessGranted##
受限制的访问 订阅存取

详细

The interaction of [PSI+] and [PIN+] factors in yeast Saccharomyces cerevisiae is known as the first evidence of prions networks. In [PIN+] cells, Rnq1p prion aggregates work as a template for Sup35p aggregation, which is essential for [PSI+] induction. No additional factors are required for subsequent Sup35p aggregation. Nevertheless, several recent reports provide data that indicate a more complex interplay between these prions. Our results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI+] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). These observations support the existence of interaction networks that converge on a strong linkage of prionogenic and prion-like proteins, and the participation of Rnq1 protein in the maintenance of prion [PSI+].

作者简介

S. Bondarev

Laboratory of Physiological Genetics, Department of Genetics and Biotechnology; Laboratory of Amyloid Biology

编辑信件的主要联系方式.
Email: stanislavspbgu@gmail.com
俄罗斯联邦, St. Petersburg, 199034; St. Petersburg, 199034

D. Likholetova

Laboratory of Physiological Genetics, Department of Genetics and Biotechnology

Email: stanislavspbgu@gmail.com
俄罗斯联邦, St. Petersburg, 199034

M. Belousov

Laboratory of Physiological Genetics, Department of Genetics and Biotechnology

Email: stanislavspbgu@gmail.com
俄罗斯联邦, St. Petersburg, 199034

G. Zhouravleva

Laboratory of Physiological Genetics, Department of Genetics and Biotechnology; Laboratory of Amyloid Biology

Email: stanislavspbgu@gmail.com
俄罗斯联邦, St. Petersburg, 199034; St. Petersburg, 199034

补充文件

附件文件
动作
1. JATS XML

版权所有 © Pleiades Publishing, Inc., 2017