NR AYHK
AU Kryndushkin,D.S.; Wickner,R.B.
TI Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae
QU Molecular Biology of the Cell 2007 Jun; 18(6): 2149-54
IA http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1877104
PT journal article; research support, n.i.h., intramural
AB The [URE3] and [PSI(+)] prions are infectious amyloid forms of Ure2p and Sup35p. Several chaperones influence prion propagation: Hsp104p overproduction destabilizes [PSI(+)], whereas [URE3] is sensitive to excess of Ssa1p or Ydj1p. Here, we show that overproduction of the chaperone, Sse1p, can efficiently cure [URE3]. Sse1p and Fes1p are nucleotide exchange factors for Ssa1p. Interestingly, deletion of either SSE1 or FES1 completely blocked [URE3] propagation. In addition, deletion of SSE1 also interfered with [PSI(+)] propagation.
MH Adenosine Triphosphatases/genetics/metabolism; Guanine Nucleotide Exchange Factors/genetics/*metabolism; HSP110 Heat-Shock Proteins/genetics/*metabolism; HSP40 Heat-Shock Proteins/genetics/metabolism; HSP70 Heat-Shock Proteins/genetics/*metabolism; Intracellular Signaling Peptides and Proteins/genetics/metabolism; Point Mutation; Prions/genetics/*metabolism; Saccharomyces cerevisiae/cytology/genetics/*metabolism; Saccharomyces cerevisiae Proteins/genetics/*metabolism
AD Dmitry Kryndushkin and Reed B. Wickner (wickner@helix.nih.gov), Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA.
SP englisch
PO USA