GTC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Genes to Cells (2009) 14, 659-668. doi:10.1111/j.1365-2443.2009.01297.x
© 2009 Blackwell Publishing or its licensors

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kurahashi, H.
Right arrow Articles by Nakamura, Y.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Kurahashi, H.
Right arrow Articles by Nakamura, Y.

Selfish prion of Rnq1 mutant in yeast

Hiroshi Kurahashi, Shoichiro Shibata, Masao Ishiwata and Yoshikazu Nakamura*

Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

[PIN+] is a prion form of Rnq1 in Saccharomyces cerevisiae and is necessary for the de novo induction of a second prion, [PSI+]. We previously isolated a truncated form of Rnq1, named Rnq1{Delta}100, as a [PSI+]-eliminating factor in S. cerevisiae. Rnq1{Delta}100 deletes the N-terminal non-prion domain of Rnq1, and eliminates [PSI+] in [PIN+] yeast. Here we found that [PIN+] is transmissible to Rnq1{Delta}100 in the absence of full-length Rnq1, forming a novel prion variant [RNQ1{Delta}100+]. [RNQ1{Delta}100+] has similar [PIN+] properties as it stimulates the de novo induction of [PSI+] and is eliminated by the null hsp104{Delta} mutation, but not by Hsp104 overproduction. In contrast, [RNQ1{Delta}100+] inherits the inhibitory activity and hampers the maintenance of [PSI+] though less efficiently than [PIN+] made of Rnq1–Rnq1{Delta}100 co-aggregates. Interestingly, [RNQ1{Delta}100+] prion was eliminated by de novo [PSI+] induction. Thus, the [RNQ1{Delta}100+] prion demonstrates selfish activity to eliminate a heterologous prion in S. cerevisiae, showing the first instance of a selfish prion variant in living organisms.


Communicated by: Hiroji Aiba

* Correspondence: nak{at}ims.u-tokyo.ac.jp







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
Copyright © 2009 by Wiley-Blackwell Publishing.