Literature DB >> 20148963

Amyloid oligomers: diffuse oligomer-based transmission of yeast prions.

Hideki Taguchi1, Shigeko Kawai-Noma.   

Abstract

Prions are infectious proteins, in which self-propagating amyloid conformations of proteins are transmitted. The budding yeast Saccharomyces cerevisiae, one of the best-studied model eukaryotes, also has prions, and thus provides a tractable model system with which to understand the mechanisms of prion phenomena. The yeast prions are protein-based heritable elements, such as [PSI(+)], in which aggregates of prion proteins are transmitted to daughter cells in a non-Mendelian manner. Although the genetic approaches preceded the yeast prion studies, recent investigations of the dynamic aspects of the prion proteins have unraveled the molecular mechanisms by which prions are propagated and transmitted. In particular, several lines of evidence have revealed that the oligomeric species of prion proteins dispersed in the cytoplasm are critical for the transmission. This review summarizes the topics on the transmissible entities of yeast prions, focusing mainly on the Sup35 protein in [PSI(+)].

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Year:  2010        PMID: 20148963     DOI: 10.1111/j.1742-4658.2010.07569.x

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  8 in total

1.  Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy.

Authors:  Hiroki Konno; Takahiro Watanabe-Nakayama; Takayuki Uchihashi; Momoko Okuda; Liwen Zhu; Noriyuki Kodera; Yousuke Kikuchi; Toshio Ando; Hideki Taguchi
Journal:  Proc Natl Acad Sci U S A       Date:  2020-03-25       Impact factor: 11.205

Review 2.  Amyloids and prions in plants: Facts and perspectives.

Authors:  K S Antonets; A A Nizhnikov
Journal:  Prion       Date:  2017-09-03       Impact factor: 3.931

Review 3.  A bipolar personality of yeast prion proteins.

Authors:  Hiroshi Kurahashi; Keita Oishi; Yoshikazu Nakamura
Journal:  Prion       Date:  2011-10-01       Impact factor: 3.931

4.  In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

Authors:  Shigeko Kawai-Noma; Chan-Gi Pack; Tomoko Kojidani; Haruhiko Asakawa; Yasushi Hiraoka; Masataka Kinjo; Tokuko Haraguchi; Hideki Taguchi; Aiko Hirata
Journal:  J Cell Biol       Date:  2010-07-19       Impact factor: 10.539

5.  Prion domains as a driving force for the assembly of functional nanomaterials.

Authors:  Weiqiang Wang; Salvador Ventura
Journal:  Prion       Date:  2020-12       Impact factor: 3.931

6.  A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions.

Authors:  Keita Oishi; Hiroshi Kurahashi; Chan-Gi Pack; Yasushi Sako; Yoshikazu Nakamura
Journal:  Microbiologyopen       Date:  2013-03-20       Impact factor: 3.139

7.  Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.

Authors:  Jennifer E Dulle; Rachel E Bouttenot; Lisa A Underwood; Heather L True
Journal:  J Cell Biol       Date:  2013-10-21       Impact factor: 10.539

8.  Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.

Authors:  Chan-Gi Pack; Yuji Inoue; Takashi Higurashi; Shigeko Kawai-Noma; Daigo Hayashi; Elizabeth Craig; Hideki Taguchi
Journal:  BMB Rep       Date:  2017-09       Impact factor: 4.778

  8 in total

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