A terminal α3-galactose modification regulates an E3 ubiquitin ligase subunit in Toxoplasma gondii.

ABSTRACT: Skp1, a subunit of E3 Skp1/Cullin-1/F-box protein ubiquitin ligases, is modified by a prolyl hydroxylase that mediates O₂ regulation of the social amoeba Dictyostelium and the parasite Toxoplasma gondii The full effect of hydroxylation requires modification of the hydroxyproline by a pentasaccharide that, in Dictyostelium, influences Skp1 structure to favor assembly of Skp1/F-box protein subcomplexes. In Toxoplasma, the presence of a contrasting penultimate sugar assembled by a different glycosyltransferase enables testing of the conformational control model. To define the final sugar and its linkage, here we identified the glycosyltransferase that completes the glycan and found that it is closely related to glycogenin, an enzyme that may prime glycog

SUBMITTER: Mandalasi M 

PROVIDER: S-EPMC7335778 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature