Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions
@article{Goto2007ProteinOI, title={Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions}, author={Masatoshi Goto}, journal={Bioscience, Biotechnology, and Biochemistry}, year={2007}, volume={71}, pages={1415 - 1427} }
Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation…
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References
SHOWING 1-10 OF 111 REFERENCES
Molecular characterization of protein O-mannosyltransferase and its involvement in cell-wall synthesis in Aspergillus nidulans.
- BiologyMicrobiology
- 2004
The results indicate that PmtA is required for the formation of a normal cell wall in Aspergillus nidulans, and indicates that protein O-glycosylation is essential for protein modification and plays important roles in eukaryotic cells.
PMT1, the gene for a key enzyme of protein O-glycosylation in Saccharomyces cerevisiae.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1993
It was observed that protein O-mannosylation in the disruptant had decreased only to about 40-50%, indicating the existence of an additional transferase which had not been measured by the in vitro enzyme assay, which led to a complete loss of in vitro mannosyltransferase activity.
The PMT gene family: protein O‐glycosylation in Saccharomyces cerevisiae is vital.
- Biology, EngineeringThe EMBO journal
- 1996
The results show that protein O‐glycosylation is essential for cell wall rigidity and cell integrity and that this protein modification, therefore, is vital for Saccharomyces cerevisiae.
O-mannosyl glycans: from yeast to novel associations with human disease.
- Biology, ChemistryCurrent opinion in structural biology
- 2003
Protein-O-glycosylation in yeast: protein-specific mannosyltransferases.
- Biology, EngineeringGlycobiology
- 1997
The results clearly indicate that the various protein O-mannosyltransferases have different specificities for protein substrates.
Roles of O-Mannosylation of Aberrant Proteins in Reduction of the Load for Endoplasmic Reticulum Chaperones in Yeast*
- BiologyJournal of Biological Chemistry
- 2004
O-Mannosylation may function as a fail-safe mechanism for the ERad by solubilizing the aberrant proteins that overflowed from the ERAD pathway and reducing the load for ER chaperones.
Protein O‐glycosylation in Saccharomyces cerevisiae: the protein O‐mannosyltransferases Pmt1p and Pmt2p function as heterodimer
- BiologyFEBS letters
- 1995
O‐Mannosylation precedes and potentially controls the N‐glycosylation of a yeast cell wall glycoprotein
- Biology, EngineeringEMBO reports
- 2003
It is shown that the Pmt4 and Pmt1/Pmt2 mannosyltransferases glycosylate different domains of the Ccw5 protein, thereby mannosyating several consecutive serine and threonine residues, and that O‐mannosylation by PMT4 precedes N‐glycosylation.