POLYAMINE OXIDASE 1 from rice (Oryza sativa) is a functional ortholog of Arabidopsis POLYAMINE OXIDASE 5

Plant Signaling & Behavior
Taibo LiuTomonobu Kusano

Abstract

POLYAMINE OXIDASE 1 (OsPAO1), from rice (Oryza sativa), and POLYAMINE OXIDASE 5 (AtPAO5), from Arabidopsis (Arabidopsis thaliana), are enzymes sharing high identity at the amino acid level and with similar characteristics, such as polyamine specificity and pH preference; furthermore, both proteins localize to the cytosol. A loss-of-function Arabidopsis mutant, Atpao5-2, was hypersensitive to low doses of exogenous thermospermine but this phenotype could be rescued by introduction of the wild-type AtPAO5 gene. Introduction of OsPAO1, under the control of a constitutive promoter, into Atpao5-2 mutants also restored normal thermospermine sensitivity, allowing growth in the presence of low levels of thermospermine, along with a concomitant decrease in thermospermine content in plants. By contrast, introduction of OsPAO3, which encodes a peroxisome-localized polyamine oxidase, into Atpao5-2 plants could not rescue any of the mutant phenotypes in the presence of thermospermine. These results suggest that OsPAO1 is the functional ortholog of AtPAO5.

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Citations

Mar 19, 2020·International Journal of Molecular Sciences·Ming-Dong ZhuYan-Mei Lv
Jan 23, 2019·BMC Evolutionary Biology·Cesar Daniel BordenaveAndrés Alberto Rodríguez
May 28, 2019·Frontiers in Plant Science·Wei WangJi-Hong Liu
Oct 22, 2020·Scientific Reports·Daniele Salvi, Paraskevi Tavladoraki
Jul 6, 2021·Physiology and Molecular Biology of Plants : an International Journal of Functional Plant Biology·G H M SagorThomas Berberich

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