Comparative acetylome analysis reveals the potential mechanism of high fat diet function in allergic disease

Modern technological lifestyles promote allergic diseases,especially food allergies.The underlying molecular mechanisms remain to be uncovered.Protein acetylation is one of the most important post-translational modifications,and it is involved in regulating multiple body metabolic processes.This study aimed to clarify the effects of a high-fat diet(HFD)on allergy risk and the underlying mechanisms.Four-week-old male C57 BL/6 J mice were randomly divided into two groups and fed a normal fat diet(NFD)or HFD for 24 weeks.Then,serum lipids were measured,and skeletal muscle was collected for acetylome analysis.Compared with the findings in the NFD group,HFD-fed mice were obese and hyperlipidemic.Acetylome analysis also revealed 32 differentially expressed proteins between the HFD and NFD groups.Among these,eight acetylated proteins were upregulated in the HFD group.In addition,13 and 11 proteins were acetylated only in the HFD group and NFD group,respectively.These proteins were mainly involved in regulating energy metabolism and mitochondrial function.This study provides information regarding the underlying molecular mechanisms by which HFD promotes allergy.

Global Lysine Acetylome Analysis of Flower Bud Development in Catalpa bungei

Lysine acetylation,a reversible and dynamic post-translational modification,plays pivotal roles in regulating many biological processes in plants.However,the information of lysine acetylation during flower development of woody angiosperm remains unclear.Herein,we identified a total of 667 lysine acetylation sites in 467 proteins in flower buds of Catalpa Bungei.The acetylated proteins were mainly involved in the pathways of carbon metabolism,glycometabolism and oxidative phosphorylation.Using functional enrichment analysis,61 and 13 acetylated proteins were involved in the glycometabolism and oxidative phosphorylation pathways,respectively.This suggests that lysine acetylated proteins play critical roles in the energy metabolism pathways.Accordingly,the protein–protein interactions were also highly enriched in the carbon metabolic pathway.Integrative analysis of lysine acetylome and transcriptome showed that transcript level changes of seven key lysine-acetylated proteins/genes involved in energy metabolism were significant different during floral transition.Importantly,compared with the normal flowering variety,the expression levels of phosphoribulokinase,phosphoenolpyruvate carboxykinase,ATP synthase and pyruvate dehydrogenase complex genes were significantly up-regulated at the stages of vegetative and transition buds during early flowering of C.bungei.These data represent the first lysine acetylome in the C.bungei flowers,and can serve as an essential basis for exploring the function of lysine acetylated proteins in the flower bud development of plants.

Multi-omics Data Reveal the Effect of Sodium Butyrate on Gene Expression and Protein Modification in Streptomyces

Streptomycetes possess numerous gene clusters and the potential to produce a large amount of natural products.Histone deacetylase(HDAC)inhibitors play an important role in the regulation of histone modifications in fungi,but their roles in prokaryotes remain poorly understood.Here,we investigated the global effects of the HDAC inhibitor,sodium butyrate(SB),on marine-derived Streptomyces olivaceus FXJ 8.021,particularly focusing on the activation of secondary metabolite biosynthesis.The antiSMASH analysis revealed 33 secondary metabolite biosynthetic gene clusters(BGCs)in strain FXJ 8.021,among which the silent lobophorin BGC was activated by SB.Transcriptomic data showed that the expression of genes involved in lobophorin biosynthesis(ge00097–ge00139)and CoA-ester formation(e.g.,ge02824),as well as the glycolysis/gluconeogenesis pathway(e.g.,ge01661),was significantly up-regulated in the presence of SB.Intracellular CoA-ester analysis confirmed that SB triggered the biosynthesis of CoA-ester,thereby increasing the precursor supply for lobophorin biosynthesis.Further acetylomic analysis revealed that the acetylation levels on 218 sites of 190 proteins were up-regulated and those on 411 sites of 310 proteins were down-regulated.These acetylated proteins were particularly enriched in transcriptional and translational machinery components(e.g.,elongation factor GE04399),and their correlations with the proteins involved in lobophorin biosynthesis were established by protein–protein interaction network analysis,suggesting that SB might function via a complex hierarchical.