Isolation of a novel protein phosphatase2C in rice and its response to gibberellin

被引:8
作者
Hossain, Md Amir [1 ,2 ]
Ahn, Chul-Hyun [1 ]
Lee, In Suk [1 ]
Jeon, Jong-Seong [3 ]
An, Gynheung [3 ]
Park, Phun Bum [1 ]
机构
[1] Univ Suwon, Dept Biosci & Biotechnol, Hwaseong, South Korea
[2] Bangladesh Agr Univ, Dept Genet & Plant Breeding, Mymensingh, Bangladesh
[3] Kyung Hee Univ, Grad Sch Biotechnol, Yongin, South Korea
关键词
Protein Phosphatase2C; alpha-amylase; GA signaling; Germination; Rice; SIGNAL-TRANSDUCTION; NEGATIVE REGULATOR; FRUIT-DEVELOPMENT; DROUGHT STRESS; GENE FAMILIES; 2C; ACID; ARABIDOPSIS; GERMINATION; EXPRESSION;
D O I
10.1016/j.bbrc.2018.07.146
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein phosphatase 2Cs (PP2Cs) have been referred to act as negative modulators of the protein kinase pathways involved in different environmental stress responses and developmental processes. In Arabidopsis, PP2Cs have been extensively studied and some are known to negatively regulate abscisic acid signaling. In rice, PP2Cs are scarcely characterized functionally. Here, we identified a novel PP2C from rice (OsPP2C34), which is highly inducible by gibberellin (GA) and expressed in various tissues. Subcellular localization analysis in maize protoplasts using a green fluorescence protein fusion vector localized OsPP2C34 to the cytosol. Genetic analysis of T-DNA insertional mutants revealed that plant height and internode length were significantly shorter in mutants than in corresponding wild types under GA treatment. The induction of the GA-inducible alpha-amylase genes RAmy3E and OsAmy was delayed in mutant plants. The substrate of OsPP2C34 was identified by immunoblotting using anti serine/threonine antibodies. A 65 kDa protein was phosphorylated in Ospp2c34-1 but dephosphorylated in the wild type during early germination stage. Overall, the present results indicated that OsPP2C34 is involved in alpha-amylase expression of GA signal transduction pathway. (C) 2018 Elsevier Inc. All rights reserved.
引用
收藏
页码:1987 / 1992
页数:6
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