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Fig. 3 | BMC Molecular and Cell Biology

Fig. 3

From: Biochemical and genetic analysis of Ecm14, a conserved fungal pseudopeptidase

Fig. 3

Ecm14 is N-glycosylated and processed by an endopeptidase in S. cerevisiae. a Yeast extracts that overexpressed Ecm14-His6 were incubated with endoglycosidase H (EndoH) and analyzed by western blotting with an anti-His6 antibody. ProEcm14 observed as a broad band at 45 kDa (likely two bands) collapses to one thin band with EndoH, and mature Ecm14 observed as two bands at 35 kDa collapses to one. b NetNGlyc 1.0 predicts there to be two N-glycosylation sites within Ecm14, on asparagines at positions 41 within the prodomain and 295 within the carboxypeptidase domain. c These asparagines, shown as yellow spheres, are both located on the surface of the Ecm14 homology model. The prodomain of Ecm14 is shown in blue, the carboxypeptidase-like domain in green, and a coordinated zinc is modeled as a red sphere

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