Conformation preserved in a weak-to-strong or strong-to-weak [PSI+] conversion during transmission to Sup35 prion variants

被引：4

作者：

Crist, Colin G. ^{[1
]}

Kurahashi, Hiroshi ^{[1
]}

Nakayashiki, Toru ^{[1
]}

Nakamura, Yoshikazu ^{[1
]}

机构：

[1] Univ Tokyo, Inst Med Sci, Dept Basic Med Sci, Minato Ku, 4-6-1 Shirokanedai, Tokyo 1088639, Japan

来源：

BIOCHIMIE | 2006年 / 88卷 / 05期

关键词：

yeast prion; Sup35; PSI+; conformational memory; oligopeptide repeats;

D O I：

10.1016/j.biochi.2005.10.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cytoplasmic [PSI+] element of budding yeast represents the prion conformation of translation release factor Sup35. Much interest lies in understanding how prions are able to generate variation in isogenic strains. Recent observations suggest that a single prion domain, PrD, is able to adopt several conformations that account for prion strains. We report novel PrD variants of Sup35 that convert weak [PSI+] to strong [PSI+], and vice versa, upon transmission from wild-type Sup35. During the transmission from wild-type Sup35 to variant Sup35s, no conformational changes were detected by proteolytic fingerprinting and the original [PSI+] strain was remembered upon return to wild-type Sup35. These findings suggest that during transmission to variant Sup35s, the [PSI+] phenotype is variable while the original conformation is remembered. A mechanism of "conformational memory" to remember specific [PSI+] conformations during transmission is proposed. (c) 2005 Elsevier SAS. All rights reserved.

引用

页码：485 / 496

页数：12

共 45 条

[1] DISTINCT PRP PROPERTIES SUGGEST THE MOLECULAR-BASIS OF STRAIN VARIATION IN TRANSMISSIBLE MINK ENCEPHALOPATHY [J].