Journal of Environmental Biology

Cloning and expression analysis of an aldehyde oxidase gene in

Arachis hygogaea L.

 

Lixia Yang, Jianhua Liang, Haihang Li and Ling Li*

Guangdong Provincial Key Lab of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou - 510631, P.R. China

(Received: October 16, 2007; Revised received: February 10, 2008; Accepted: March 05, 2008)

Abstract: Aldehyde oxidase (AO) plays important role in plant hormone biosynthetic pathways, such as abscisic acid (ABA) and indole-3-acetic acid (IAA). The enzyme catalyzes the last step of the pathways. In this study, a full-length cDNA encoding an aldyhyde oxidase was cloned and sequenced from leaves of peanut by RT-PCR, RACE-PCR and genomic DNA walking methods. The full-length cDNA, designated as Arachis hygogaea L. aldehyde oxidase1 (AhAO1), consists of an open reading frame of 4131bp, a 326 bp 5? untranslated region and a 128 bp 3?? untranslated region including a poly (A) tail of 21 nucleotides. The gene encodes a polypeptide of 1377 amino acids with a calculated molecular weight of 150 kDa and an isoelectric point (pI) of 6.99. Analysis of amino acid sequence of AhAO1 shows that it had 61%, 59% and 55% identity with the AOs from tomato, Arabidopsis and maize, respectively. The peanut AO polypeptide contains consensus sequences for iron-sulfur centers and a molybdenum cofactor (MoCo)-binding domain. Semi-quantitative RT-PCR analysis showed that AhAO1 expression was higher in leaves than in roots of peanut.

Key words: Cloning, Expression, Aldehyde oxidase, Arachis hypogaea L.

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