Identification of the actual coding region for polyamine oxidase 6 from rice (OsPAO6) and its partial characterization

Abstract

Polyamines (PA) in plant play roles in growth and development and in responses to environmental stresses. The family of polyamine oxidases (PAO) contributes to a balanced homeostasis of PAs catalyzing two different reactions, terminal catabolic (TC) and back-conversion (BC) pathway, in PA catabolism. From the seven PAOs encoded by the rice genome (OsPAO1–OsPAO7) OsPAO6 could so far not be characterized due to failure in obtaining the coding cDNA based on accessions in the genomic databases. We report cloning and characterization of the correct OsPAO6 cDNA with a length of 1,742 bp. The 1,491 bp long open reading frame codes for a 497-amino acid protein from nine exons. The protein which has 92% identity to OsPAO7 localizes to plasma membrane.