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Proteomic Analysis of Lysine Acetylation and succinylation in pogostemon cablin

ABSTRACT: By the combination of affinity enrichment and high-resolution LC-MS/MS analysis, large-scale lysine acetylome analysis was performed. Altogether, 6,925 lysine acetylation sites in 2,526 protein groups were identified. Intensive bioinformatic analysis was then carried out to annotate those identified lysine acetylated targets in response to drug treatment, including GO annotation, domain annotation, subcellular localization, KEGG pathway annotation, functional cluster analysis, etc. Based on the results, further studies following the lysine acetylome analysis were suggested

INSTRUMENT(S): Q Exactive

ORGANISM(S): Pogostemon Cablin

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Jones Macke

LAB HEAD: Likai Chen

PROVIDER: PXD015567 | Pride | 2019-12-11

REPOSITORIES: Pride

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Publications

Global analysis of lysine succinylation in patchouli plant leaves.

Wang Xiaobing X Chen Xiuzhen X Li Junren J Zhou Xuanxuan X Liu Yanting Y Zhong Liting L Tang Yun Y Zheng Hai H Liu Jiyun J Zhan Ruoting R Chen Likai L

Horticulture research 20191201

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 (<i>P. cablin</i> (Blanco) Benth., Lamiaceae) is a globally important industrial plant and medicinal herb. In the present study, lysine succinylome analysis was carried out in patchouli ...[more]

PMID: 31814986

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Proteomic Analysis of Lysine Succinylation in oryza sativa

Project description:By the combination of affinity enrichment and high-resolution LC-MS/MS analysis, large-scale lysine succinylome analysis was performed. Altogether, 742 lysine succinylation sites in 382 protein groups were identified. Intensive bioinformatic analyses were then carried out to annotate those identified lysine succinylated targets in response to drug treatment, including GO annotation, domain annotation, subcellular localization, KEGG pathway annotation, functional cluster analysis, etc. Based on the results, further studies following the lysine succinylome analysis were suggested

2018-10-26 | PXD005582 | Pride

Global PTM Mapping for Lysine 2-hydroxyisobutyrylation in one Oryza Sativa Japonica sample

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2018-10-26 | PXD005986 | Pride

Global lysine acetylome analysis of Picea asperata somatic 1 embryos during partial desiccation

Project description:By the combination of affinity enrichment and high-resolution LC-MS/MS analysis, large-scale lysine acetylome analysis was performed in picea asperata. Altogether, 1,360 lysine acetylation sites in 717 protein groups were identified. Intensive bioinformatic analysis was then carried out to annotate those lysine acetylated targets, including protein annotation, functional classification, functional enrichment, etc.

2018-10-26 | PXD005042 | Pride

Succinylation proteome analysis of seedling leaves of Bd21

Project description:Protein lysine succinylation, an emerging protein post-translational modification widespread among microbiology, animals and plants, represents an important regulator of cellular processes. In our study, we took the first succinylation proteome analysis in the seedling leaves of Bd21 to draw a schematic map. With high accuracy nano LC-MS/MS combined with affinity purification, a total of 605 succinylated peptides in 323 proteins were identified and were implicated in various molecular functions and cellular biological processes. More than half (53.4%) of the proteins only have one lysine succinylated site. These identified proteins are involved in a variety of cellular functions such as amino acids transport/metabolism, post-translational modification, translation/ribosomal structure and lipid metabolism, especially energy and carbohydrate metabolism via GO, conservation analysis, protein interaction network and other bioinformatics analysis. Motif-X analysis of the succinylation sites identified fourteen significantly enriched succinylation motifs (-Ksucc-----K-, -Ksucc------G- etc) for the first time in plants and will provide possible succinylation binding locus for future studies. Secondary structure analysis showed that the succinylation sites occurred predominantly in alpha helix and coil structures which similar with acetylation. 155 (59.2%) of the homologous succinylated proteins were also identified in other three species (E. coli, S. cerevisiae and H. sapiens). 119 (45.4%) succinylated proteins and 115 (19%) sites were also to be acetylated at the same time. Our succinylated protein data set provides a promising starting point for further functional analysis of succinylation in B. distachyon, which could facilitate the elucidation of the entire metabolic network in the model monocot plant.

2018-10-26 | PXD003428 | Pride

A Qualitative Proteome-wide Lysine Succinylation Profiling of Tea Revealed Its Involvement in Primary Metabolism

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2022-02-23 | PXD011717 | Pride

Systematic analysis of the lysine acetylome in Beauveria bassiana

Project description:Lysine acetylation emerging as a ubiquitous and conserved posttranslational modification plays an important regulatory role in almost every aspect of eukaryotes and prokaryotes. To gain insight into the nature, extent and biological function of lysine acetylation in Beauveria bassiana, a filamentous entomopathogenic fungus, we used immunoaffinity-based acetyl-lysine peptide enrichment integrated with high resolution mass spectrometry to comprehensively characterize lysine acetylated proteins in this fungus. Here we identified a total of 283 proteins with 464 acetylated sites, representing the first acetylproteome reported to date in filamentous fungi. Bioinformatics analysis of this acetylome showed that the acetylated proteins are involved in a wide range of cellular functions, such as metabolism, transcription, and exhibit diverse subcellular localizations. Enrichment of molecular function, biological process, and KEGG pathway implied that identified acetylated proteins of B. bassiana were very important in chromatin organization, ribosome, nucleosome assembly, carbon metabolism, and biosynthesis of secondary metabolites. Moreover, we matched five conserved lysine acetylated motifs containing of KacY, KacH, KacF, FxKac, KacxxxxK and one specific motif KacW in B. bassiana. Taken together, our acetylome analysis revealed a surprising breadth of cellular processes affected by lysine acetylation and also furnishes some fresh intervention nodes for the rational improvement of the friednly entomopathogenic fungus.

2017-11-02 | PXD003682 | Pride

Identification of lysine succinylome and acetylome in vancomycin-intermediate Staphylococcus aureus XN108

Project description:In this study, we detected the first lysine succinylome and acetylome in a vancomycin-intermediate S. aureus (VISA) strain, XN108.Furthermore,Comparative analysis of the protein succinylation and acetylation between XN108-ΔcobB and XN108-WT strain was conducted on the basis of quantitative detection of both protein expression and protein modification

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Tomato (Solanum lycopersicum) lysine succinylation LC-MS/MS

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Succinylome and acetylome analyses of Staphylococcus aureusSuccinylome and acetylome analyses of Staphylococcus aureus

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