Domain structure and function of ?-1,3-glucanase from bacillus circulans KA-304, an enzyme essential for degrading basidiomycete cell walls
Bacillus circulans KA-304 ?-1,3-glucanase (Agl-KA) includes an N-terminal discoidin domain (DS1), a carbohydrate binding module family 6 (CB6), threonine and proline repeats (TPs), a second discoidin domain (DS2), an uncharacterized conserved domain (UCD), and a C-terminal catalytic domain. Domain d...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
2014
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| Online Access: | http://www.scopus.com/inward/record.url?eid=2-s2.0-84876368787&partnerID=40&md5=f9df5d04d8a89af084a97ee9e86837ce http://cmuir.cmu.ac.th/handle/6653943832/7254 |
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| Institution: | Chiang Mai University |
| Language: | English |
| Summary: | Bacillus circulans KA-304 ?-1,3-glucanase (Agl-KA) includes an N-terminal discoidin domain (DS1), a carbohydrate binding module family 6 (CB6), threonine and proline repeats (TPs), a second discoidin domain (DS2), an uncharacterized conserved domain (UCD), and a C-terminal catalytic domain. Domain deletion enzymes lacking DS1, CB6, and DS2 exhibited lower ?-1,3-glucan-hydrolyzing and -binding activities than the wild type, Agl-KA. An ?-1,3-glucan binding assay with fluorescent protein fusion proteins indicated that DS1, CB6, and DS2 bound to ?-1,3-glucan and fungal cell walls, and that binding efficiency was increased by their combined action. In contrast, UCD did not exhibit any ?-1,3-glucan-binding activity. A dramatic decrease in protoplast formation in the Schizophyllum commune mycelium was observed given only a DS1 deletion. An Agl-KA with deletion DS1, CB6, and DS2 produced no protoplasts. These results indicate that the combined actions of DS1, CB6, and DS2 contributed to increased cell-wall binding and were indispensable for efficient Agl-KA cell-wall degradation. |
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