Defining the function of SUMO system in pod development and abiotic stresses in Peanut

Yiyang Liu,Jiao Zhu,Xuejie Zhang,Yan Han,Sheng Sun,Guowei Li,Feng Cui,Zhenying Peng,Shubo Wan

doi:10.1186/s12870-019-2136-9

Abstract

BackgroundPosttranslational modification of proteins by small ubiquitin like modifier (SUMO) proteins play an important role during the developmental process and in response to abiotic stresses in plants. However, little is known about SUMOylation in peanut (Arachis hypogaea L.), one of the world’s major food legume crops. In this study, we characterized the SUMOylation system from the diploid progenitor genomes of peanut, Arachis duranensis (AA) and Arachis ipaensis (BB).ResultsGenome-wide analysis revealed the presence of 40 SUMO system genes in A. duranensis and A. ipaensis. Our results showed that peanut also encodes a novel class II isotype of the SCE1, which was previously reported to be uniquely present in cereals. RNA-seq data showed that the core components of the SUMOylation cascade SUMO1/2 and SCE1 genes exhibited pod-specific expression patterns, implying coordinated regulation during pod development. Furthermore, both transcripts and conjugate profiles revealed that SUMOylation has significant roles during the pod development. Moreover, dynamic changes in the SUMO conjugates were observed in response to abiotic stresses.ConclusionsThe identification and organization of peanut SUMO system revealed SUMOylation has important roles during stress defense and pod development. The present study will serve as a resource for providing new strategies to enhance agronomic yield and reveal the mechanism of peanut pod development.

Highlights

Posttranslational modification of proteins by small ubiquitin like modifier (SUMO) proteins play an important role during the developmental process and in response to abiotic stresses in plants
We scanned the genome of the diploid ancestors: Arachis. duranensis (AA genome) and Arachis. ipaensis (BB genome) available in PeanutBase using BLASTP and TBLASTN
The amino acid sequences of the known Arabidopsis SUMO, E1, E2, E3, and SUMO protease protein were used as queries

Summary

Introduction

Posttranslational modification of proteins by small ubiquitin like modifier (SUMO) proteins play an important role during the developmental process and in response to abiotic stresses in plants. The small ubiquitin-like modifier (SUMO) peptide to protein substrates (SUMOylation) is a major posttranslational regulatory process in eukaryotes [3]. SUMO precursors are processed by SUMO-specific cysteine (Cys) proteases (ULP, ubiquitin-like protein protease) with. SCE can conjugate SUMO to the substrate proteins, resulting in the formation of an isopeptide linkage between the carboxyl-terminal Gly of SUMO and the ε-amino group of a lysine (Lys) residue within the substrate [1]. The SUMO ligases play important roles in vivo to determine substrate specificity and the extent of SUMOylation [4].

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Results

Conclusion