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KMID : 1160220140420020167
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Mycobiology
2014 Volume.42 No. 2 p.167 ~ p.173
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Cloning and Molecular Characterization of β-1,3- Glucan Synthase from Sparassis crispa
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Yang Yun Hui
Kang Hyeon-Woo
Ro Hyeon-Su
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Abstract
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A β-glucan synthase gene was isolated from the genomic DNA of polypore mushroom Sparassis crispa, whichreportedly produces unusually high amount of soluble β-1,3-glucan (β-glucan). Sequencing and subsequent open reading frameanalysis of the isolated gene revealed that the gene (5,502 bp) consisted of 10 exons separated by nine introns. The predictedmRNA encoded a β-glucan synthase protein, consisting of 1,576 amino acid residues. Comparison of the predicted proteinsequence with multiple fungal β-glucan synthases estimated that the isolated gene contained a complete N-terminus but waslacking approximately 70 amino acid residues in the C-terminus. Fungal β-glucan synthases are integral membrane proteins,containing the two catalytic and two transmembrane domains. The lacking C-terminal part of S. crispa β-glucan synthase wasestimated to include catalytically insignificant transmembrane α-helices and loops. Sequence analysis of 101 fungal β-glucansynthases, obtained from public databases, revealed that the β-glucan synthases with various fungal origins were categorized intocorresponding fungal groups in the classification system. Interestingly, mushrooms belonging to the class Agaricomycetes werefound to contain two distinct types (Type I and II) of β-glucan synthases with the type-specific sequence signatures in the loopregions. S. crispa β-glucan synthase in this study belonged to Type II family, meaning Type I β-glucan synthase is expected to bediscovered in S. crispa. The high productivity of soluble β-glucan was not explained but detailed biochemical studies on thecatalytic loop domain in the S. crispa β-glucan synthase will provide better explanations.
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KEYWORD
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β-Glucan, Cell wall, Glucan synthase, Sparassis crispa
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