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PMID:22492205

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Citation

Pasikowska, M, Palamarczyk, G and Lehle, L (2012) The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast. Glycobiology 22:939-47

Abstract

Rot1 is an essential yeast protein originally shown to be implicated in such diverse processes such as β-1,6-glucan synthesis, actin cytoskeleton dynamics or lysis of autophagic bodies. More recently also a role as a molecular chaperone has been discovered. Here, we report that Rot1 interacts in a synthetic manner with Ost3, one of the nine subunits of the oligosaccharyltransferase (OST) complex, the key enzyme of N-glycosylation. The deletion of OST3 in the rot1-1 mutant causes a temperature sensitive phenotype as well as sensitivity toward compounds interfering with cell wall biogenesis such as Calcofluor White, caffeine, Congo Red and hygromycin B, whereas the deletion of OST6, a functional homolog of OST3, has no effect. OST activity in vitro determined in membranes from rot1-1ost3Δ cells was found to be decreased to 45% compared with wild-type membranes, and model glycoproteins of N-glycosylation, like carboxypeptidase Y, Gas1 or dipeptidyl aminopeptidase B, displayed an underglycosylation pattern. By affinity chromatography, a physical interaction between Rot1 and Ost3 was demonstrated. Moreover, Rot1 was found to be involved also in the O-mannosylation process, as the glycosylation of distinct glycoproteins of this type were affected as well. Altogether, the data extend the role of Rot1 as a chaperone required to ensure proper glycosylation.

Links

PubMed Online version:10.1093/glycob/cws068

Keywords

Dimethylallyltranstransferase/metabolism; Endoplasmic Reticulum/metabolism; Gene Knockout Techniques; Glycosylation; Hexosyltransferases/genetics; Hexosyltransferases/metabolism; Mannose/metabolism; Mannosyltransferases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Membrane Proteins/physiology; Microbial Viability; Microsomes/enzymology; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Phenotype; Protein Binding; Protein Processing, Post-Translational; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/growth & development; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/genetics; Saccharomyces cerevisiae Proteins/metabolism; Saccharomyces cerevisiae Proteins/physiology

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