Application of GFP-labeling to study prions in yeast.
Fluorescent live cell imaging has recently been used in numerous studies to examine prions in yeast. These fluorescence studies take advantage of the fact that unlike the normally folded form, the misfolded amyloid form of the prion protein is aggregated. The studies have used fluorescence to identify new prions, to study the transmission of prion from mother to daughter, and to understand the role of molecular chaperones in this transmission. The use of fluorescence imaging complements the more standard methods used to study prion propagation. This review discusses the various studies that have taken advantage of fluorescence imaging technique particularly in regard to understanding the transmission and curing of the [PSI(+)], the prion form of the translation termination factor Sup35p.
Greene
Lois E
LE
Laboratory of Cell Biology, NHLBI, NIH, Bethesda, MD 20892-0301, USA. greenel@helix.nih.gov
Park
Yang-Nim
YN
Masison
Daniel C
DC
Eisenberg
Evan
E
D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology*; D049452:Green Fluorescent Proteins / Q000235:genetics*; D008856:Microscopy, Fluorescence / Q000379:methods*; D018832:Molecular Chaperones; D010454:Peptide Termination Factors / Q000235:genetics / Q000502:physiology; D011328:Prions / Q000235:genetics / Q000502:physiology*; D011993:Recombinant Fusion Proteins / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000502:physiology
D005656:Fungal Proteins; D018832:Molecular Chaperones; D010454:Peptide Termination Factors; D011328:Prions; D011993:Recombinant Fusion Proteins; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D049452:Green Fluorescent Proteins