Systematic analysis of the lysine acetylome in Fusarium graminearum

Zhou, Shanyue; Yang, Qiwen; Yin, Changfa; Liu, Lin; Liang, Wenxing

doi:10.1186/s12864-016-3361-3

Cited by 44 publications

(78 citation statements)

References 52 publications

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“…Emerging evidence shows that lysine acetylation plays a major role in metabolism regulation and frequently occurs in almost all enzymes in the central carbon metabolism (Wang et al ., ), so we investigated the acetylation of metabolic enzymes in A. flavus by mapping acetylated proteins to Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways (Table S5). Consistent with previous findings on lysine acetylation (Henriksen et al ., ; Li et al ., ; Zhou et al ., ), a large proportion of metabolic enzymes involved in central metabolism were acetylated, such as enzymes involved in the pentose phosphate pathway, glycolysis/gluconeogenesis and citric acid cycle (Fig. ), implying that lysine acetylation may regulate cellular metabolic processes at multiple levels.…”

Section: Resultsmentioning

confidence: 99%

“…In addition, the proportion of identified acetylated proteins to the total protein (5.39%) in A. flavus is much lower than that in S. cerevisiae (17.93%) (Henriksen et al ., ), but close to filamentous fungi C. albicans (5.28%) (Zhou et al ., ) and B. cinerea (5.82%) (Lv et al ., ). The protein–protein interaction results also showed that the acetylated proteins are involved in many metabolic processes, which are consistent with the results of acetylomic analysis in the plant pathogenic fungi F. graminearum (Zhou et al ., ) and Phytophthora sojae (Li et al ., ).…”

Section: Discussionmentioning

confidence: 99%

“…In this study, we found that nearly all enzymes involved in the TCA cycle are targets of lysine acetylation (Fig. ), which is similar to the previous studies on acetylated proteomics in various organisms, such as M. tuberculosis (Liu et al ., ), B. cinerea (Lv et al ., ), H. capsulatum (Xie et al ., ), F. graminearum (Zhou et al ., ) and P. sojae (Li et al ., ). As a major product in TCA cycle, acety‐CoA is also the initial substrate for aflatoxin biosynthesis (Amaike and Keller, ).…”

Section: Discussionmentioning

confidence: 99%

“…The same approach has since been employed to analyse the other prokaryotic model organisms, including Bacillus subtilis (Kim et al ., ), Mycobacterium tuberculosis (Liu et al ., ), Vibrio cholerae (Jers et al ., ) and Streptococcus pneumoniae (Liu et al ., ). In addition, the acetylome of fungi such as Saccharomyces cerevisiae (Henriksen et al ., ), Candida albicans (Zhou et al ., ), Beauveria bassiana (Wang et al ., ), Botrytis cinerea (Lv et al ., ), Fusarium graminearum (Zhou et al ., ) and Histoplasma capsulatum (Xie et al ., ) have also been reported, and most acetylated proteins are found to play crucial roles in central metabolism, protein synthesis, cell cycle and virulence. In Aspergillus flavus , a total of 1383 acetylated sites in 652 proteins that are involved in central metabolism, transcriptional regulation and secondary metabolism were identified (Lv, ).…”

Section: Introductionmentioning

confidence: 99%

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Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Guang

Yue

Ren

et al. 2019

Environmental Microbiology

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Summary Aspergillus flavus is a pathogenic fungus that produces carcinogenic aflatoxins, posing a great threat to crops, animals and humans. Lysine acetylation is one of the most important reversible post‐translational modifications and plays a vital regulatory role in various cellular processes. However, current information on the extent and function of lysine acetylation and aflatoxin biosynthesis in A. flavus is limited. Here, a global acetylome analysis of A. flavus was performed by peptide pre‐fractionation, pan‐acetylation antibody enrichment and liquid chromatography–mass spectrometry. A total of 1313 high‐confidence acetylation sites in 727 acetylated proteins were identified in A. flavus. These acetylation proteins are widely involved in glycolysis/gluconeogenesis, pentose phosphate pathway, citric acid cycle and aflatoxin biosynthesis. AflO (O‐methyltransferase), a key enzyme in aflatoxin biosynthesis, was found to be acetylated at K241 and K384. Deletion of aflO not only impaired conidial and sclerotial developments, but also dramatically suppressed aflatoxin production and pathogenicity of A. flavus. Further site‐specific mutations showed that lysine acetylation of AflO could also result in defects in development, aflatoxin production and pathogenicity, suggesting that acetylation plays a vital role in the regulation of the enzymatic activity of AflO in A. flavus. Our findings provide evidence for the involvement of lysine acetylation in various biological processes in A. flavus and facilitating in the elucidation of metabolic networks.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Guang

Yue

Ren

et al. 2019

Environmental Microbiology

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“…of K ac sitesNo. of K ac proteins% of acetylationReferencesYeasts Y. lipolytica 64723163142822.1This study S. cerevisiae 54042878105919.6Henriksen et al (2012)Fungi P. sojae 19,027219711506.0Li et al (2016) B. cinerea 1638915829545.82Lv et al (2016) F. graminearum 13,3345773642.73Zhou et al (2016)Bacteria B. amyloliquefaciens 38113268125432.9Liu et al (2016) M. tuberculosis 4034112865816.3Xie et al (2015) Synechocystis sp.367277651314.0Mo et al (2015) V. parahemolyticus 4823141365613.6Pan et al (2014) S. reseosporus 689111436679.7Liao et al (2014) E. coli 414410703498.4…”

Section: Discussionmentioning

confidence: 96%

Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica

et al. 2017

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Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes. Yarrowia lipolytica, an oleaginous yeast, is considered as a model for bio-oil production due to its ability to accumulate a large amount of lipids. However, the function of lysine acetylation in this organism is elusive. Here, we performed a global acetylproteome analysis of Y. lipolytica ACA-DC 50109. In total, 3163 lysine acetylation sites were identified in 1428 proteins, which account for 22.1% of the total proteins in the cell. Fifteen conserved acetylation motifs were detected. The acetylated proteins participate in a wide variety of biological processes. Notably, a total of 65 enzymes involved in lipid biosynthesis were found to be acetylated. The acetylation sites are distributed in almost every type of conserved domains in the multi-enzymatic complexes of fatty acid synthetases. The provided dataset probably illuminates the crucial role of reversible acetylation in oleaginous microorganisms, and serves as an important resource for exploring the physiological role of lysine acetylation in eukaryotes.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0393-2) contains supplementary material, which is available to authorized users.

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Acetylome analysis of the feline small intestine following Toxoplasma gondii infection

et al. 2020

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Toxoplasma gondii is a protozoan parasite capable of infecting a large number of warm-blooded animals and causes serious health complications in immunocompromised patients. T. gondii infection of the feline small intestine is critical for the completion of the life cycle and transmission of T. gondii. Protein acetylation is an important posttranslational modification, which plays roles in the regulation of various cellular processes. Therefore, understanding of how T. gondii reprograms the protein acetylation status of feline definitive host can help to thwart the production and spread of T. gondii. Here, we used affinity enrichment and high-resolution liquid chromatography with tandem mass spectrometry to profile the alterations of the acetylome in cat small intestine 10 days after infection by T. gondii Prugniuad (Pru) strain. Our analysis showed that T. gondii induced significant changes in the acetylation of proteins in the cat intestine. We identified 2606 unique lysine acetylation sites in 1357 acetylated proteins. The levels of 334 acetylated peptides were downregulated, while the levels of 82 acetylated peptides were increased in the infected small intestine. The proteins with differentially acetylated peptides were particularly enriched in the bioenergeticsrelated processes, such as tricarboxylic acid cycle, oxidative phosphorylation, and oxidation-reduction. These results provide the first baseline of the global acetylome of feline small intestine following T. gondii infection and should facilitate further analysis of the role of acetylated protein in the pathogenesis of T. gondii infection in its definitive host.

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Systematic analysis of the lysine acetylome in Fusarium graminearum

Cited by 44 publications

References 52 publications

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica

Acetylome analysis of the feline small intestine following Toxoplasma gondii infection

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