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. 2020 Oct 16;9:e61886. doi: 10.7554/eLife.61886

Figure 5. Relative abundance of (a) simple and modular ascarosides and (b) simple and modular glucosides in the endo-metabolome of Cbr-glo-1 mutants relative to wild-type C. briggsae.

n.d., not detected. (c) Model for modular metabolite assembly. CEST proteins (membrane-bound in the LROs, red) mediate attachment of building blocks from diverse metabolic pathways to glucose scaffolds and peroxisomal β-oxidation-derived ascarosides via ester and amide bonds. Some of the resulting modular ascarosides may undergo additional peroxisomal β-oxidation following activation by acs-7 (Dolke et al., 2019).

Figure 5—source data 1. Source data for Figure 5a–b.
Attached as a separate file.

Figure 5.

Figure 5—figure supplement 1. Gut granules in C. briggsae.

Figure 5—figure supplement 1.

(a) C. briggsae WT AF16 has gut granules similar to C. elegans which are also both birefringent and easily tagged by Lysotracker Red (see arrows). Gut granule loss is evident in both (b) Cbr-glo-1(sy1382) and (c) Cbr-glo-1(sy1383).