Analysis of ANS structures and molecular evolution in Rosaceae

Abstract

Anthocyanidin Synthase (ANS) is a key rate-limiting enzyme involves in the biosynthesis of anthocyanin. Notably, anthocyanin contents of Rosaceae have a significant impact on its economic value as major economic crops. Thus, the role of ANS in the regulation of anthocyanin contents in the Rosaceae family is worthy of investigation. Since the characterizations and expression pattern of ANS in the Rosaceae family are largely unknown so far, a systematic analysis is required to extend current understanding. Using the bioinformatics methods, we performed comprehensive bioinformatic analysis for the ANS amino acid sequences of 11 major Rosaceae species, which shared a high degree of similarity and identity, and also clustered closely in the phylogenetic analysis. Through homology modeling, 11 Rosaceae species ANS were divided into two groups: one group with similar structures to AtANS and the other with similar structures to AtACO2. Further protein-ligand docking showed that most ANS might be involved in the anthocyanin synthesis. This study found that ANS from 11 Rosaceae species shared highly similar characteristics, protein structures, and binding characteristics, helping increase the understanding of ANS evolution in Rosaceae fruits and providing supports for studies in the regulation of anthocyanin biosynthesis of Rosaceae plants.