2013 Fiscal Year Final Research Report
Functional analysis of alpha-1,3-glucanase: the enzyme participates in fungal cell-wall hydrolysis
| Project/Area Number |
24780085
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied microbiology
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| Research Institution | Yamagata University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | α-1,3-グルカナーゼ / 細胞壁 |
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| Research Abstract |
Bacillus circulans KA-304 alpha-1,3-glucanase (Agl-KA) is a multi-domain enzyme, and it includes N-terminal DS1, CB6, DS2, UCD, and C-terminal catalytic domain. To clarify the role of these domains, we constructed several domain deletion enzymes and GFP-fusion proteins. As the results, DS1, CB6, and DS2 domain bound to alpha-1,3-glucan and fungal cell-wall, and that binding efficiency was increased by combined action. The findings indicate that DS1, CB6, and DS2 are novel alpha-1,3-glucan binding domain.
In order to obtain the further information on structure and function of alpha-1,3-glucanases, we purified and characterized a novel alpha-1,3-glucanase (Agl-FH1) of Paenibacillus glycanilyticus FH11. Although the properties of Agl-FH1 were almost the same as those of Agl-KA, the amino acid sequence of catalytic domain of Agl-FH1 showed approximately 20% identity to that of Agl-KA. The results may be beneficial to clarify the catalytic mechanism of the enzyme in the future.
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Research Products
(10 results)
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[Journal Article] Functional analysis of theα-1,3-glucan synthase genes agsA and agsB in Aspergillus nidulans : agsB is the majorα-1,3-glucan synthase in this fungus2013
Author(s)
Yoshimi A., Sano M., Inaba A., Kokubun Y., Fujioka T., Mizutani O., Hagiwara D., Fujikawa T., Nishimura M., Yano S., Kasahara S., Shimizu K., Yamaguchi M., Kawakami K., Abe K.
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Journal Title
PLoS One
Volume: 8(1)
Pages: e54893
Peer Reviewed
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