The First Whole-Cell Proteome- and Lysine-Acetylome-Based Comparison between <i>Trichophyton rubrum</i> Conidial and Mycelial Stages

Xu, Xingye; Liu, Tao; Yang, Jian; Liu, Bo; Wang, Lingling; Jin, Qi

doi:10.1021/acs.jproteome.7b00793

Cited by 29 publications

(37 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MS/MS data were searched against the UniProt N. tabacum database concatenated with the reverse decoy database. 55 The fixed modification was carbamidomethyl on Cys, and the variable modifications were Gly-Gly modification on lysine (K) and oxidation on methionine. The maximal missed cleavage of trypsin/P was 4.…”

Section: Methodsmentioning

confidence: 99%

Comprehensive Proteomic Analysis of Lysine Ubiquitination in Seedling Leaves of Nicotiana tabacum

et al. 2020

View full text Add to dashboard Cite

Lysine ubiquitination, a widely studied posttranslational modification, plays vital roles in various biological processes in eukaryotic cells. Although several studies have examined the plant ubiquitylome, no such research has been performed in tobacco, a model plant for molecular biology. Here, we comprehensively analyzed lysine ubiquitination in tobacco ( Nicotiana tabacum ) using LC–MS/MS along with highly sensitive immune-affinity purification. In total, 964 lysine-ubiquitinated (K ub ) sites were identified in 572 proteins. Extensive bioinformatics studies revealed the distribution of these proteins in various cellular locations, including the cytoplasm, chloroplast, nucleus, and plasma membrane. Notably, 25% of the K ub proteins were located in the chloroplast of which 21 were enzymatically involved in important pathways, that is, photosynthesis and carbon fixation. Western blot analysis indicated that TMV infection can cause changes in ubiquitination levels. This is the first comprehensive proteomic analysis of lysine ubiquitination in tobacco, illustrating the vital role of ubiquitination in various physiological and biochemical processes and representing a valuable addition to the existing landscape of lysine ubiquitination.

show abstract

Section: Methodsmentioning

confidence: 99%

Comprehensive Proteomic Analysis of Lysine Ubiquitination in Seedling Leaves of Nicotiana tabacum

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Different modified proteins in the aflatoxin biosynthesis clusters (AflM, AflK, AflP and AflO) were identified in our study, when compared with Lv's result (AflA, AflB). In some species, such as Trichophyton rubrum (Xu et al ., ), B. bassiana (Cai et al ., ) and M. tuberculosis (Yang et al ., ), differences in acetylation‐modified proteins and sites were detected when compared to previous studies. Thus, we believe that the difference in acetylation modification is also common in A. flavus .…”

Section: Discussionmentioning

confidence: 99%

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

Guang

Yue

Ren

et al. 2019

Environmental Microbiology

View full text Add to dashboard Cite

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.

show abstract

“…To verify the protein expression levels obtained by TMT analysis, 20 differentially abundant proteins (unique peptides≥ 2, fold change > 1.3 or < 0.77) were randomly chosen based on the TMT results and further quantified by the PRM assay according to Xu’s method [ 55 ] at Jingjie PTM-Biolab Co., Ltd. (Hangzhou, China).…”

Section: Methodsmentioning

confidence: 99%

Comparative Physiological and Proteomic Analysis Reveals Different Involvement of Proteins during Artificial Aging of Siberian Wildrye Seeds

Xiong

Liu²,

Zhao

et al. 2020

Plants

View full text Add to dashboard Cite

Seed aging has an important effect on the germplasm preservation and industrialized production of Siberian wildrye (Elymus sibiricus) in the Qinghai-Tibet Plateau. However, so far its underlying molecular mechanisms still largely remain unknown. To shed light on this topic, one-year stored seeds of E. sibiricus were exposed to artificial aging treatments (AAT), followed by seed vigor characteristics and physiological status monitoring. Then global proteomics analysis was undertaken by the tandem mass tags (TMT) technique, and the proteins were quantified with liquid chromatography-tandem mass spectrometry on three aging time points (0 h, 36 h and 72 h). Finally, we verified the expression of related proteins by parallel reaction monitoring (PRM). Our results demonstrated that the seed vigor decreased remarkably in response to artificial aging, but the relative ion-leakage and malondialdehyde content, superoxide anion and hydrogen peroxide showed the opposite situation. Proteomic results showed that a total of 4169 proteins were identified and quantified. Gene Ontology (GO) analysis and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis indicated that a series of key pathways including carbohydrate metabolism, lipid metabolism, and antioxidant activity were severely damaged by aging treatments. Numerous key proteins such as glyceraldehyde triphosphate glyceraldehyde dehydrogenase, succinate dehydrogenase, lipoxygenase, peroxidase, glutathione-s-transferase and late embryogenesis abundant proteins were significantly down-regulated. However, the up-regulation of the heat shock protein family has made a positive contribution to oxidative stress resistance in seeds. This study provides a useful catalog of the E. sibiricus proteomes with insights into the future genetic improvement of seed storability.

show abstract

The First Whole-Cell Proteome- and Lysine-Acetylome-Based Comparison between Trichophyton rubrum Conidial and Mycelial Stages

Cited by 29 publications

References 46 publications

Comprehensive Proteomic Analysis of Lysine Ubiquitination in Seedling Leaves of Nicotiana tabacum

Comprehensive Proteomic Analysis of Lysine Ubiquitination in Seedling Leaves of Nicotiana tabacum

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

Comparative Physiological and Proteomic Analysis Reveals Different Involvement of Proteins during Artificial Aging of Siberian Wildrye Seeds

Contact Info

Product

Resources

About