Lysine succinylation is a novel,naturally occurring posttranslational modification(PTM)in living organisms.Global lysine succinylation identification has been performed at the proteomic level in various species;howeve...Lysine succinylation is a novel,naturally occurring posttranslational modification(PTM)in living organisms.Global lysine succinylation identification has been performed at the proteomic level in various species;however,the study of lysine succinylation in plant species is relatively limited.Patchouli plant(P.cablin(Blanco)Benth.,Lamiaceae)is a globally important industrial plant and medicinal herb.In the present study,lysine succinylome analysis was carried out in patchouli plants to determine the potential regulatory role of lysine succinylation in patchouli growth,development,and physiology.The global succinylation sites and proteins in patchouli plants were screened with an immunoprecipitation affinity enrichment technique and advanced mass spectrometry-based proteomics.Several bioinformatic analyses,such as function classification and enrichment,subcellular location predication,metabolic pathway enrichment and protein−protein interaction networking,were conducted to characterize the functions of the identified sites and proteins.In total,1097 succinylation sites in 493 proteins were detected in patchouli plants,among which 466 succinylation sites in 241 proteins were repeatedly identified within three independent experiments.The functional characterization of these proteins indicated that the tricarboxylic acid(TCA)cycle,oxidative phosphorylation,photosynthesis processes,and amino acid biosynthesis may be regulated by lysine succinylation.In addition,these succinylated proteins showed a wide subcellular location distribution,although the chloroplast and cytoplasm were the top two preferred cellular components.Our study suggested the important role of lysine succinylation in patchouli plant physiology and biology and could serve as a useful reference for succinylation studies in other medicinal plants.展开更多
基金support for this research was provided in part by a grant from Project 81803657 supported by the National Natural Science Foundation of Chinathe Guangdong Education department Key Promotion Platform Construction Project,Lingnan Key Laboratory of Chinese Medicine Resources Ministry of Education(2014KTSPT016)+1 种基金special funds for the Construction of Traditional Chinese Medicine in Guangdong Province(No.20181075)the earmarked fund for Guangdong Education Department Innovation Strong School Project(No.E1-KFD015181K28/2017KQNCX039).
文摘Lysine succinylation is a novel,naturally occurring posttranslational modification(PTM)in living organisms.Global lysine succinylation identification has been performed at the proteomic level in various species;however,the study of lysine succinylation in plant species is relatively limited.Patchouli plant(P.cablin(Blanco)Benth.,Lamiaceae)is a globally important industrial plant and medicinal herb.In the present study,lysine succinylome analysis was carried out in patchouli plants to determine the potential regulatory role of lysine succinylation in patchouli growth,development,and physiology.The global succinylation sites and proteins in patchouli plants were screened with an immunoprecipitation affinity enrichment technique and advanced mass spectrometry-based proteomics.Several bioinformatic analyses,such as function classification and enrichment,subcellular location predication,metabolic pathway enrichment and protein−protein interaction networking,were conducted to characterize the functions of the identified sites and proteins.In total,1097 succinylation sites in 493 proteins were detected in patchouli plants,among which 466 succinylation sites in 241 proteins were repeatedly identified within three independent experiments.The functional characterization of these proteins indicated that the tricarboxylic acid(TCA)cycle,oxidative phosphorylation,photosynthesis processes,and amino acid biosynthesis may be regulated by lysine succinylation.In addition,these succinylated proteins showed a wide subcellular location distribution,although the chloroplast and cytoplasm were the top two preferred cellular components.Our study suggested the important role of lysine succinylation in patchouli plant physiology and biology and could serve as a useful reference for succinylation studies in other medicinal plants.
