Fig. 3.
Variants in drxIR1 interval do not alter the biophysical properties of polyQ aggregates. a FRAP analysis. The soluble Q40::YFP protein recovered rapidly (triangles), while aggregated protein (circles) in both Q40Bristol and drxIR1;Q40 backgrounds does not recover. Data are mean ± SD. b PolyQ40 aggregates in native extract from drxIR1;Q40 animals remain resistant to 5% SDS. Aggregated proteins fail to enter the native gel, remaining in the wells (shown). Native extracts containing the fibrillar GFP::UNC-54 protein were used as controls. c The increased aggregation phenotype in animals carrying the drxlR1 interval does not depend on the amyloid-specific modifier moag-4 (mid-L4 animals; YA animals are shown in Suppl. Fig. 3B). Data are mean ± SD, three independent experiments. Thirty-eight to 46 animals per condition. Data were analyzed by ANOVA followed by Bonferroni’s multiple comparisons test, ****P < 0.0001. d Aggregation of a different amyloid protein, Aβ1-40::CFP, in unaffected by the drxlR1 locus. Shown are confocal stacks, arrows point to aggregates, and asterisks indicate Aβ1-40::CFP accumulating in the nuclei of the muscle cells. Scale bar, 10 μm. e The shorter polyQ expansion (Q35::YFP) exhibits both the increased susceptibility of the head muscle cells and the accelerated overall aggregation in animals carrying the drxlR1 interval. Shown are stereo micrographs; arrows point to some of the aggregates. D1Ad, day 1 adults