Fig. 3

Protein aggregation and longevity. We used multiCM to analyze insoluble fractions of C. elegans proteins [16]. a Analysis of mass-spectrometry data indicates that in the hsf-1 strain (short-lived) highly enriched proteins (class HSF 4/4) are more aggregation prone than those less enriched (class HSF1 1/4). b In the daf-2 strain (long-lived), highly enriched proteins (DAF2 4/4) show lower aggregation propensities than the ones poorly enriched (DAF2 1/4). In these calculations, the insoluble fraction of the strains is divided into 4 equal sets containing proteins with fold enrichments > 1 with respect to wild type worm and ranked from low (1/4) to high (4/4)  [green dots indicate row vs column enrichments]. c Using the cleverGO algorithm, we analyzed proteins present in the hsf-1 strain (i.e., reported in HSF-1 4/4 and not in DAF-2 4/4) and found enrichments in metabolic pathways, oxidative stress response and mitochondrial function. Links to the analyses are at http://www.tartaglialab.com/cs_multi/confirm/757/9e1710f579/ and http://www.tartaglialab.com/cs_multi/confirm/758/95acfc44da/