- THIS ARTICLE
- Full Text (Rapid PDF)
-
All Versions of this Article:
genetics.105.048660v1
172/2/827 most recent - Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Shkundina, I. S
- Articles by Ter-Avanesyan, M. D
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Shkundina, I. S
- Articles by Ter-Avanesyan, M. D
doi:10.1534/genetics.105.048660
A more recent version of this article appeared on February 1, 2006.
REGULAR RESEARCH PAPERS |
The Role of the N-Terminal Ologopeptide Repeats of the Yeast Sup35 Prion Protein in Propagation and Transmission of Prion Variants
Irina S Shkundina 1, Vitaly V Kushnirov 1, Mick F Tuite 2 and Michael D Ter-Avanesyan 1*
1 Cardiology Research Center
2 University of Kent
* To whom correspondence should be addressed. E-mail: mdter{at}cardio.ru.
Submitted on July 22, 2005
Revised on August 15, 2005
Accepted on 20 October 2005
The cytoplasmic [PSI+] determinant of Saccharomyces cerevisiae is the prion form of the Sup35 protein. Oligopeptide repeats within the Sup35 N-terminal domain (PrD) presumably are required for the stable [PSI+] inheritance that in turn involves fragmentation of Sup35 polymers by the chaperone Hsp104. The nonsense suppressor [PSI+] phenotype can vary in efficiency probably due to different inheritable Sup35 polymer structures. Here, we study the ability of Sup35 mutants with various deletions of the oligopeptide repeats to support [PSI+] propagation. We define the minimal region of the Sup35-PrD necessary to support [PSI+] as amino acids 1-64, which includes the first two repeats, though a longer fragment, 1-83, is required to maintain weak [PSI+] variants. Replacement of wild-type Sup35 with deletion mutants decreases the strength of the [PSI+] phenotype. However, with one exception, reintroducing the wild-type Sup35 restores the original phenotype. Thus, the specific prion fold defining the [PSI+] variant can be preserved by the mutant Sup35 protein despite the change of phenotype. Co-expression of wild type and mutant Sup35 containing three, two, one or no oligopeptide repeats causes variant-specific [PSI+] elimination. These data suggest that [PSI+] variability is primarily defined by differential folding of the Sup35-PrD oligopeptide repeats region.
Key Words: Sup35, [PSI+], oligopeptide repeats, prion strains, yeast
This article has been cited by other articles:
 |
|
 |
|
  J. Dong, J. D. Bloom, V. Goncharov, M. Chattopadhyay, G. L. Millhauser, D. G. Lynn, T. Scheibel, and S. Lindquist Probing the Role of PrP Repeats in Conformational Conversion and Amyloid Assembly of Chimeric Yeast Prions J. Biol. Chem., November 23, 2007; 282(47): 34204 - 34212. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Kawai-Noma, S. Ayano, C.-G. Pack, M. Kinjo, M. Yoshida, K. Yasuda, and H. Taguchi Dynamics of yeast prion aggregates in single living cells. Genes Cells, September 1, 2006; 11(9): 1085 - 1096. [Abstract] [Full Text] [PDF]
|
|