Functional Properties of a Cysteine Proteinase from Pineapple Fruit with Improved Resistance to Fungal Pathogens in Arabidopsis thaliana
文献类型: 外文期刊
作者: Wang, Wei 1 ; Zhang, Lu 3 ; Guo, Ning 1 ; Zhang, Xiumei 2 ; Zhang, Chen 1 ; Sun, Guangming 2 ; Xie, Jianghui 2 ;
作者机构: 1.Anhui Agr Univ, Sch Life Sci, Anhui Key Lab Plant Genet & Breeding, Hefei 230036, Peoples R China
2.Chinese Acad Trop Agr Sci CATAS, Inst China Southern Subtrop Crop Res, Key Lab Trop Fruit Biol, Minist Agr, Guangzhou 524091, Guangdong, Peoples R China
3.Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, Guangzhou 510006, Guangdong, Peoples R China
关键词: Ananas comosus;cysteine proteinase;gene expression;proteolytic properties;resistance
期刊名称:MOLECULES ( 影响因子:4.411; 五年影响因子:4.587 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: 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.
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