Cloning and expression analysis of an aldehyde oxidase gene in Arachis hygogaea L.

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 oxidase 1 (AhAO1), consists of an open reading frame of 4131 bp, 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 (pl) 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.