An oxidative and salinity stress induced peroxisomal ascorbate peroxidase from Avicennia marina:: Molecular and functional characterization

被引：32

作者：

Kavitha, Kumaresan ^{[1
]}

Venkataraman, Gayatri ^{[1
]}

Parida, Ajay ^{[1
]}

机构：

[1] MS Swaminathan Res Fdn, Taramani Inst Area, Chennai 600113, Tamil Nadu, India

来源：

PLANT PHYSIOLOGY AND BIOCHEMISTRY | 2008年 / 46卷 / 8-9期

关键词：

ascorbate peroxidase; Avicennia marina; green fluorescent protein; hydrogen peroxide; peroxisome; subcellular localization;

D O I：

10.1016/j.plaphy.2008.05.008

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

APX (EC, 1. 11. 1. 11) has a key role in scavenging ROS and in protecting cells against their toxic effects in algae and higher plants. A cDNA encoding a peroxisomal ascorbate peroxidase, Am-pAPX1, was isolated from salt stressed leaves of Avicennia marina (Forsk.) Vierh. by EST library screening and its expression in the context of various environmental stresses was investigated. Am-pAPX1 contains an ORF of 286 amino acids coding for a 31.4 kDa protein. The C-terminal region of the Ani-pAPX1 ORF has a putative transmembrane domain and a peroxisomal targeting signal (RKKMK), suggesting peroxisomal localization. The peroxisomal localization of Am-pAPX1 was confirmed by stable transformation of the GFP-(Ala)(10)-Am-pAPX1 fusion in tobacco. RNA blot analysis revealed that Am-pAPX1 is expressed in response to salinity (NaCl) and oxidative stress (high intensity light, hydrogen peroxide application and excess iron). The isolated genomic clone of Am-PAPX1 was found to contain nine exons. A fragment of 1616 bp corresponding to the 5' upstream region of Am-pAPX1 was isolated by TAIL-PCR. In silico analysis of this sequence reveals the presence of putative light and abiotic stress regulatory elements. (C) 2008 Elsevier Masson SAS. All rights reserved.

引用

页码：794 / 804

页数：11

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