Genome-Wide Identification and Characterization of the ANS Gene Family in Pomegranate (Punica granatum L.)

Anthocyanidin Synthase (ANS) is a key enzyme in the later stages of the anthocyanin biosynthetic pathway, and its role is to convert colorless leucoanthocyanidins to colored anthocyanidins. In this study, a total of 75 members of the pomegranate ANS family were identified and divided into four groups (Group I, Group II, Group III and Group IV) based on evolutionary relationships. The 75 ANS gene family members were unevenly distributed on seven of the eight chromosomes of pomegranate. The results of the physical and chemical property analysis showed that 93.33% of the proteins were acidic proteins, 6.67% were alkaline proteins, 28% of the proteins were stable proteins and 72% were unstable proteins. Protein secondary structure analysis showed that alpha-Spiral and irregular curl are the main structural elements. Analysis of the conserved structural domains of the proteins showed that all 75 ANS family members contained one DIOX-N subfamily structural domain and one 2OG-FeII_Oxy subfamily structural domain. The results of subcellular localization showed that all 75 ANS family members of pomegranate were localized in the cytoplasm. Analysis of the transcriptome data showed that the expression of the pomegranate ANS genes were variety-specific and period-specific.

Automated summary

In this study, 75 members of the pomegranate ANS family were identified and categorized into four groups based on evolutionary relationships. These genes were unevenly distributed on seven chromosomes and most proteins were acidic and unstable. The proteins had alpha-spiral and irregular curl as the main structural elements, and conserved domains such as DIOX-N subfamily and 2OG-FeII_Oxy subfamily. The expression of pomegranate ANS genes was specific to variety and growth period.