Abstract

BackgroundUbiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities. However, the E3 family and their functions are yet to be identified in the fruit of peach.ResultsIn this study, genome-wide identification, classification and characterization of the E3 ligase genes within the genome of peach (Prunus persica) was carried out. In total, 765 E3 (PpE3) ligase genes were identified in the peach genome. The PpE3 ligase genes were divided into eight subfamilies according to the presence of known functional domains. The RBX subfamily was not detected in peach. The PpE3 ligase genes were not randomly distributed among the 8 chromosomes, with a greater concentration on the longer chromosomes. The primary mode of gene duplication of the PpE3 ligase genes was dispersed gene duplication (DSD). Four subgroups of the BTB subfamily never characterized before were newly identified in peach, namely BTBAND, BTBBL, BTBP and BTBAN. The expression patterns of the identified E3 ligase genes in two peach varieties that display different types of fruit softening (melting flesh, MF, and stony hard, SH) were analyzed at 4 different stages of ripening using Illumina technology. Among the 765 PpE3 ligase genes, 515 (67.3%) were expressed (FPKM > 1) in the fruit of either MF or SH during fruit ripening. In same-stage comparisons, 231 differentially expressed genes (DEGs) were identified between the two peach cultivars. The number of DEGs in each subfamily varied. Most DEGs were members of the BTB, F-box, U-box and RING subfamilies. PpE3 ligase genes predicted to be involved in ethylene, auxin, or ABA synthesis or signaling and DNA methylation were differentially regulated. Eight PpE3 ligase genes with possible roles in peach flesh texture and fruit ripening were discussed.ConclusionsThe results of this study provide useful information for further understanding the functional roles of the ubiquitin ligase genes in peach. The findings also provide the first clues that E3 ligase genes may function in the regulation of peach ripening.

Highlights

  • Ubiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities

  • The findings provide the first clues that E3 ligase genes may function in the regulation of peach ripening

  • Identification and chromosomal distribution of E3 ubiquitin ligase genes in peach In peach, 765 PpE3 ligase genes were identified through BLAST analysis using protein sequences from Arabidopsis and grape against the peach genome database (Additional file 1: Table S1)

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Summary

Introduction

Ubiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities. The ubiquitin/26S proteasome pathway in eukaryotes affects most aspects of growth and development [1] through the regulated degradation of proteins. The ubiquitin/26S proteasome pathway consists of three key enzymes, namely an E1 (the ubiquitin-activating enzyme), an E2 (the ubiquitin-conjugating enzyme) and an E3 (the ubiquitin ligase). An E3 protein is responsible for selecting and transferring the E2-bound ubiquitin to the target protein. The number of E1s, E2s and E3s varies greatly among various plants. E3 proteins are the most numerous components within the ubiquitin/26S proteasome pathway, due to their role in interacting with the multitude of targets in the plant

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