Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase/N-acety lglucosaminyltransferase in a plant pathogen

• Published in: Glycobiology (Oxford) Vol. 29; no. 10; pp. 705 - 714
• Main Authors: van der Wel, Hanke, Gas-Pascual, Elisabet, West, Christopher M
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 20.09.2019
• Subjects: Cytoplasm - enzymology; Cytoplasm - genetics; Dictyostelium - genetics; Editor's Choice; F-Box Proteins - genetics; Glucosamine - analogs & derivatives; Glucosamine - genetics; Glucosamine - metabolism; Glycosylation; Hydroxylation - genetics; Microbial Biology; N-Acetylglucosaminyltransferases - genetics; N-Acetylglucosaminyltransferases - metabolism; Original; Oxygen - metabolism; Prolyl Hydroxylases - genetics; Prolyl Hydroxylases - metabolism; Proteasome Endopeptidase Complex - genetics; Proteasome Endopeptidase Complex - metabolism; Protein Isoforms - genetics; Protein Isoforms - metabolism; Pythium - genetics; Pythium - pathogenicity; S-Phase Kinase-Associated Proteins - genetics; S-Phase Kinase-Associated Proteins - metabolism; SKP Cullin F-Box Protein Ligases - genetics; Ubiquitination - genetics; E3 ubiquitin ligase; plant pathogen; glycosyltransferase; prolyl hydroxylase; Pythium ultimum

Abstract Skp1 is hydroxylated by an O2-dependent prolyl hydroxylase (PhyA) that contributes to O2-sensing in the social amoeba Dictyostelium and the mammalian pathogen Toxoplasma gondii. HO-Skp1 is subject to glycosylation and the resulting pentasaccharide affects Skp1 conformation in a way that inf...