AtPAP2, a Unique Member of the PAP Family, Functions in the Plasma Membrane

• Main Authors: Qingqing Sun, Jinyu Li, Wenzhen Cheng, Huihong Guo, Xiaomin Liu, Hongbo Gao
• Format: Article
• Language: English
• Published: MDPI AG 2018-05-01
• Series: Genes
• Subjects: purple acid phosphatase; secretory pathway; transmembrane domain; phosphorus nutrition; carbon metabolism; phylogenetic analysis
• Online Access: http://www.mdpi.com/2073-4425/9/5/257

Purple acid phosphatases (PAPs) play various physiological roles in plants. AtPAP2 was previously shown to localize to both chloroplasts and mitochondria and to modulate carbon metabolism in Arabidopsis. Over-expression of AtPAP2 resulted in faster growth and increased biomass in several plant species, indicating its great potential for crop improvement of phosphate use and yield. Here, we studied the localization of AtPAP2 by transient expression in tobacco leaves. The results showed AtPAP2 was localized to the plasma membrane through the secretory pathway, which is different from previous studies. We also found that AtPAP2 had a close relationship with fungal PAP2-like proteins based on phylogenetic analysis. In addition, the C-terminal transmembrane domain conserved in land plants is unique among other AtPAPs except AtPAP9, which is a close homolog of AtPAP2. Taken together, our results provide information for further study of AtPAP2 in understanding its special function in crop improvement.