Zhenpan Liu , Liyuan Lu , Yang Sun , Yue Zhang , Dongsheng Li , Wenzhong You

Liaoning Economic Forest Research Institute, Dalian, 116031, China
Author    Correspondence author
Genomics and Applied Biology, 2023, Vol. 14, No. 1   doi: 10.5376/gab.2023.14.0001
Received: 08 Aug., 2022    Accepted: 15 Feb., 2023    Published: 14 Mar., 2023

This article was first published in Molecular Plant Breeding in Chinese, and here was authorized to translate and publish the paper in English under the terms of Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Liu Z.P., Lu L.Y., Sun Y., Zhang Y., Li D.S., and You W.Z., 2023, Characteristics of LDOX gene structure analysis and construction of protein interaction network in Actinidia arguta, Genomics and Applied Biology, 14(1): 1-11 (doi: 10.5376/gab.2023.14.0001)

The purpose of this study is to reveal the structure and function of the leucoanthocyanidin dioxygenase (LDOX) gene in Actinidia arguta. Bioinformatics methods were used to analyze the LDOX nucleotide and amino acid sequences of Actinidia arguta, construct the protein interaction network of LDOX gene, and conduct GO and KEGG functional annotation analysis. The results showed that there were 10 conserved motifs in Actinidia arguta, which was closely related to Vaccinium corymbosum, Lonicera japonica and Daucus carota. Cis-regulated elements were mainly involved in ABA signaling pathways, responding to drought response, anaerobic induction, gibberellic acid, auxin response factor, MeJA response, low temperature response, and photostimulus response. Physical and chemical properties and structural analysis of LDOX showed that it was hydrophilic protein, and no signal peptide and transmembrane structural regions were found, mainly including Ser phosphorylation sites (13), Thr phosphorylation sites (12) and Tyr phosphorylation sites (6). There were two O-glycosylation sites (Thr⁴ and Thr³²³) and Asn¹⁰⁷of N- glycosylation sites at residues ranging from 107 to 109. There was a domain structure conservative in 48-347 bp was 20G-FeⅡ Oxy. The secondary structure main random coil (43.10%). There was a certain interaction between LDOX and proteins such as F3H, UFGT, FLS and PAL, which involved in flavonoid biosynthesis and metabolism process that plays an important role in plant-type vacuole membrane, and regulates the function of catalytic activity and redox active molecule. LDOX gene was highly conserved and plays an important regulatory role in progesterone pathway, which provides a theoretical basis for further research on the functional mechanism of LDOX gene in Actinidia arguta.

Actinidia arguta; LDOX; Structure function; Protein interaction