Extended Data Fig. 4: Sis1 requires Ssa1 and ATP for its binding to Sc4 amyloid.
From: Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system
a, Representative time-lapse TIRF images from Supplementary Video 3 showing interactions between Sc4 amyloid-STELLA650 and Ssa1-Alexa488. Sc4 amyloid-STELLA650 (red) was observed after various combinations of 2 μM Ssa1-Alexa488 (cyan) and 0.5 μM Sis1 with a distinct status of ATP were mixed and flowed. Images were acquired every 10 sec. Scale bar, 3 μm. b, Representative time-lapse TIRF images showing interactions between Sc4 amyloid-STELLA650 and Sis1-Cy3, after Sc4 amyloid-STELLA650, 0.5 μM Sis1-Cy3 and 2 μM Ssa1 with ATP or ATPγS were mixed and flowed. Images were acquired every 10 sec. Scale bar, 3 μm. c, Kinetics of accumulation of Sis1-Cy3 fluorescence on Sc4 amyloid in the presence or absence of Sis1 with ATP or ATPγS. All data were averaged from 3 independent fibers (n = 3) in 1 observation for each condition. Data are presented as mean values +/− S.D.