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Functional Properties of a Cysteine Proteinase from Pineapple Fruit with Improved Resistance to Fungal Pathogens in Arabidopsis thaliana

by Wei Wang 1,2,†, Lu Zhang 3,†, Ning Guo 1,†, Xiumei Zhang 2, Chen Zhang 1, Guangming Sun 2 and Jianghui Xie 2,*
1
Anhui Key Laboratory of Plant Genetic & Breeding, School of Life Science, Anhui Agricultural University, 130 Changjiang West Road, Hefei 230036, China
2
Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture, Institute of China Southern Subtropical Crop Research, Chinese Academy of Tropical Agricultural Sciences (CATAS), Zhanjiang 524091, Guangzhou, China
3
State Key Laboratory of Biocontrol, School of Life Sciences, SunYat-sen University, 510006 Guangzhou, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2014, 19(2), 2374-2389; https://doi.org/10.3390/molecules19022374
Received: 3 December 2013 / Revised: 19 January 2014 / Accepted: 13 February 2014 / Published: 21 February 2014
In plant cells, many cysteine proteinases (CPs) are synthesized as precursors in the endoplasmic reticulum, and then are subject to post-translational modifications to form the active mature proteinases. They participate in various cellular and physiological functions. Here, AcCP2, a CP from pineapple fruit (Ananas comosus L.) belonging to the C1A subfamily is analyzed based on the molecular modeling and homology alignment. Transcripts of AcCP2 can be detected in the different parts of fruits (particularly outer sarcocarps), and gradually increased during fruit development until maturity. To analyze the substrate specificity of AcCP2, the recombinant protein was overexpressed and purified from Pichia pastoris. The precursor of purified AcCP2 can be processed to a 25 kDa active form after acid treatment (pH 4.3). Its optimum proteolytic activity to Bz-Phe-Val-Arg-NH-Mec is at neutral pH. In addition, the overexpression of AcCP2 gene in Arabidopsis thaliana can improve the resistance to fungal pathogen of Botrytis cinerea. These data indicate that AcCP2 is a multifunctional proteinase, and its expression could cause fruit developmental characteristics of pineapple and resistance responses in transgenic Arabidopsis plants. View Full-Text
Keywords: Ananas comosus; cysteine proteinase; gene expression; proteolytic properties; resistance Ananas comosus; cysteine proteinase; gene expression; proteolytic properties; resistance
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Wang, W.; Zhang, L.; Guo, N.; Zhang, X.; Zhang, C.; Sun, G.; Xie, J. Functional Properties of a Cysteine Proteinase from Pineapple Fruit with Improved Resistance to Fungal Pathogens in Arabidopsis thaliana. Molecules 2014, 19, 2374-2389.

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