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http://140.128.103.80:8080/handle/310901/23228
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Title: | Cloning and expression of pathogenesis-related protein 4 from jelly fig (Ficus awkeotsang Makino) achenes associated with ribonuclease, chitinase and anti-fungal activities |
Authors: | Lu, H.-C., Lin, J.-H., Chua, A.C.N., Chung, T.-Y., Tsai, I.-C., Tzen, J.T.C., Chou, W.-M. |
Contributors: | Department of Food Science, Tunghai University |
Keywords: | Achene;Anti-fungal;Ficus awkeotsang;Pathogenesis-related protein 4;Pericarp;Ribonuclease |
Date: | 2012 |
Issue Date: | 2013-06-11T09:04:19Z (UTC)
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Abstract: | A cDNA fragment (FaPR4) encoding a class I pathogenesis-related protein 4 (PR-4) from Ficus awkeotsang was obtained by PCR cloning. Plant PR-4s were grouped into class I and II, differing by the presence of ChtBD and hinge. The predicted mature FaPR4 comprises N-terminal chitin-binding domain (ChtBD), hinge, Barwin domain and C-terminal extension. FaPR4-C, an N-terminal truncated form of FaPR4, was designed to mimic the structural feature of class II PR-4s. FaPR4 and FaPR4-C were over-expressed in yeast Pichia pastoris, and both recombinants exhibited RNase and anti-fungal activities. To our knowledge, it is the first report that FaPR4, a member of class I PR-4s has RNase activity as class II. FaPR4 possesses better anti-fungal activities toward Fusarium oxysporum and Sclerotium rolfsii than FaPR4-C. Heat-treated FaPR4 remained RNase and anti-fungal activities; while heat-treated FaPR4-C lost those activities. Therefore, ChtBD of FaPR4 may not only contribute to its anti-fungal but also improve the thermal stability of protein. It also implied the correlation of RNase activity with anti-fungal activity of FaPR4-C. Furthermore, FaPR4 was detected to have weak but significant chitinase activity, and its chitinase activity was reduced after heat treatment. The chitinase activity by FaPR4-C was much lower than FaPR4. ? 2012 Elsevier Masson SAS. |
Relation: | Plant Physiology and Biochemistry 56 , pp. 1-13 |
Appears in Collections: | [食品科學系所] 期刊論文
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