2013 Fiscal Year Final Research Report
Biosynthetic pathway and physiological role of pyruvylated galactose-containing oligosaccharides in fission yeast.
| Project/Area Number |
23380204
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Kyushu University |
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Principal Investigator |
TAKEGAWA Kaoru 九州大学, (連合)農学研究科(研究院), 教授 (50197282)
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| Project Period (FY) |
2011-11-18 – 2014-03-31
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| Keywords | 分裂酵母 / 糖鎖 / ガラクトース / ピルビン酸 / 糖タンパク質 |
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| Research Abstract |
In the fission yeast Schizosaccharomyces pombe, galactose residues are transferred to N- and O-linked oligosaccharides of glycoproteins by galactosyltransferases in the lumen of the Golgi apparatus. Cell surface glycoproteins play a key role in flocculation and filamentous invasive growth in yeasts. We identified fission yeast gsf2+, encoding a flocculin that binds to galactose residues located on cell surface glycoconjugates. Flocculation and invasive growth of S. pombe is tightly controlled by gsf2+ expression. MADS-box transcription factor Mbx2 regulates nonsexual flocculation by inducing gsf2+ expression. S. pombe appears to have a unique galactose-specific recognition system in which Gsf2p/flocculin plays an essential role in mediating cell-cell interactions. Furthermore, we characterized a putative S. pombe pyruvyltransferase, Pvg1p, and the recombinant Pvg1p transferred pyruvyl residues from phosphoenolpyruvate specifically to beta-linked galactose.
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[Journal Article] gfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and A. fumigatus2013
Author(s)
Komachi Y, Hatakeyama S, Motomatsu H, Futagami T, Kinzjakina K, Sorbado P, Ekino K, Takegawa K, Goto M, Nomura Y, and Oka T
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Journal Title
Mol Microbiol
Volume: 90(5)
Pages: 1054-1073
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