Cloning and expression of pathogenesis-related protein 4 from jelly fig (Ficus awkeotsang Makino) achenes associated with ribonuclease, chitinase and anti-fungal activities

Copyright © 2012 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 56(2012) vom: 05. Juli, Seite 1-13
1. Verfasser: Lu, Hsi-Chi (VerfasserIn)
Weitere Verfasser: Lin, Jia-Hui, Chua, Anna C N, Chung, Tse-Yu, Tsai, I-Chun, Tzen, Jason T C, Chou, Wing-Ming
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Antifungal Agents DNA, Complementary Plant Proteins pathogenesis-related proteins, plant Chitin 1398-61-4 RNA 63231-63-0 mehr... Ribonucleases EC 3.1.- Chitinases EC 3.2.1.14
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100 1 |a Lu, Hsi-Chi  |e verfasserin  |4 aut 
245 1 0 |a Cloning and expression of pathogenesis-related protein 4 from jelly fig (Ficus awkeotsang Makino) achenes associated with ribonuclease, chitinase and anti-fungal activities 
264 1 |c 2012 
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500 |a Date Completed 27.09.2012 
500 |a Date Revised 30.09.2020 
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500 |a Citation Status MEDLINE 
520 |a Copyright © 2012 Elsevier Masson SAS. All rights reserved. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Antifungal Agents  |2 NLM 
650 7 |a DNA, Complementary  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a pathogenesis-related proteins, plant  |2 NLM 
650 7 |a Chitin  |2 NLM 
650 7 |a 1398-61-4  |2 NLM 
650 7 |a RNA  |2 NLM 
650 7 |a 63231-63-0  |2 NLM 
650 7 |a Ribonucleases  |2 NLM 
650 7 |a EC 3.1.-  |2 NLM 
650 7 |a Chitinases  |2 NLM 
650 7 |a EC 3.2.1.14  |2 NLM 
700 1 |a Lin, Jia-Hui  |e verfasserin  |4 aut 
700 1 |a Chua, Anna C N  |e verfasserin  |4 aut 
700 1 |a Chung, Tse-Yu  |e verfasserin  |4 aut 
700 1 |a Tsai, I-Chun  |e verfasserin  |4 aut 
700 1 |a Tzen, Jason T C  |e verfasserin  |4 aut 
700 1 |a Chou, Wing-Ming  |e verfasserin  |4 aut 
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773 1 8 |g volume:56  |g year:2012  |g day:05  |g month:07  |g pages:1-13 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2012.04.004  |3 Volltext 
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