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

TitleAn oxidative and salinity stress induced peroxisomal ascorbate peroxidase from Avicennia marina: Molecular and functional characterization
Publication TypeJournal Article
Year of Publication2008
AuthorsKavitha K, Venkataraman G, Parida A
JournalPlant Physiology and Biochemistry
Start Page794
End page804
Date Published05/2008
KeywordsHydrogen peroxide, Peroxisome, Subcellular localization
Abstract

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 Am-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 50 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.

http://www.sciencedirect.com/science/article/pii/S0981942808000867

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