scholarly journals Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylated Proteins in Fusarium oxysporum

2021 ◽  
Vol 12 ◽  
Author(s):  
Hengwei Qian ◽  
Lulu Wang ◽  
Xianliang Ma ◽  
Xingling Yi ◽  
Baoshan Wang ◽  
...  

Protein lysine 2-hydroxyisobutyrylation (Khib), a new type of post-translational modification, occurs in histones and non-histone proteins and plays an important role in almost all aspects of both eukaryotic and prokaryotic living cells. Fusarium oxysporum, a soil-borne fungal pathogen, can cause disease in more than 150 plants. However, little is currently known about the functions of Khib in this plant pathogenic fungus. Here, we report a systematic analysis of 2-hydroxyisobutyrylated proteins in F. oxysporum. In this study, 3782 Khib sites in 1299 proteins were identified in F. oxysporum. The bioinformatics analysis showed that 2-hydroxyisobutyrylated proteins are involved in different biological processes and functions and are located in diverse subcellular localizations. The enrichment analysis revealed that Khib participates in a variety of pathways, including the ribosome, oxidative phosphorylation, and proteasome pathways. The protein interaction network analysis showed that 2-hydroxyisobutyrylated protein complexes are involved in diverse interactions. Notably, several 2-hydroxyisobutyrylated proteins, including three kinds of protein kinases, were involved in the virulence or conidiation of F. oxysporum, suggesting that Khib plays regulatory roles in pathogenesis. Moreover, our study shows that there are different Khib levels of F. oxysporum in conidial and mycelial stages. These findings provide evidence of Khib in F. oxysporum, an important filamentous plant pathogenic fungus, and serve as a resource for further exploration of the potential functions of Khib in Fusarium species and other filamentous pathogenic fungi.

1998 ◽  
Vol 258 (6) ◽  
pp. 599-607 ◽  
Author(s):  
M. Okuda ◽  
K. Ikeda ◽  
F. Namiki ◽  
K. Nishi ◽  
T. Tsuge

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Shoude Zhang ◽  
Lei Shan ◽  
Qiao Li ◽  
Xia Wang ◽  
Shiliang Li ◽  
...  

During the past decades, a number of studies have demonstrated multiple beneficial health effects of green tea. Polyphenolics are the most biologically active components of green tea. Many targets can be targeted or affected by polyphenolics. In this study, we excavated all of the targets of green tea polyphenolics (GTPs) though literature mining and target calculation and analyzed the multiple pharmacology actions of green tea comprehensively through a network pharmacology approach. In the end, a total of 200Homo sapienstargets were identified for fifteen GTPs. These targets were classified into six groups according to their related disease, which included cancer, diabetes, neurodegenerative disease, cardiovascular disease, muscular disease, and inflammation. Moreover, these targets mapped into 143 KEGG pathways, 26 of which were more enriched, as determined though pathway enrichment analysis and target-pathway network analysis. Among the identified pathways, 20 pathways were selected for analyzing the mechanisms of green tea in these diseases. Overall, this study systematically illustrated the mechanisms of the pleiotropic activity of green tea by analyzing the corresponding “drug-target-pathway-disease” interaction network.


1998 ◽  
Vol 88 (1) ◽  
pp. 30-32 ◽  
Author(s):  
H. C. Kistler ◽  
C. Alabouvette ◽  
R. P. Baayen ◽  
S. Bentley ◽  
D. Brayford ◽  
...  

2017 ◽  
Vol 18 (4) ◽  
pp. 1377-1384
Author(s):  
FAJAR RAHMAH NURAINI ◽  
RATNA SETYANINGSIH ◽  
ARI SUSILOWATI

Nuraini FR, Setyaningsih R, Susilowati A. 2017. Screening and characterization of endophytic fungi as antagonistic agents toward Fusarium oxysporum on eggplant (Solanum melongena). Biodiversitas 18: 1377-1384. Fusarium oxysporum is a soil borne pathogenic fungus that causes wilt disease in members of the family Solanaceae including the eggplant (Solanum melongena L.). One approach to resolving the problem of wilt disease in eggplant is to find endophytic microbes with antagonistic activity against F. oxysporum. The study reported here aimed to isolate such endophytic fungal antagonists from growing eggplants, to determine their antagonistic mechanisms, and to identify them. Samples of pathogenic fungi from diseased plants, assumed to be F. oxysporum, were obtained from the Laboratory of Plant Pests and Diseases of the Faculty of Agriculture, Universitas Sebelas Maret Surakarta. These were used to evaluate the antagonistic potential of endophytic fungi obtained from healthy eggplants in Dawung Village, Matesih, Karanganyar, Central Java. Specimens of various plant parts were collected from the healthy eggplants. The surfaces of these samples were sterilized for four minutes to remove contaminants, and then crushed excisions were cultured on a potato dextrose agar (PDA) medium. Antagonistic tests between endophytic and pathogenic fungi used the agar plug diffusion technique. Identification of fungi isolates was carried out on the basis of morphological characteristics. Six endophytic fungi isolated had antagonist activity against F. oxysporum. The antagonistic mechanism of FEB1, FEB2, FEB5 and FED1 was competition; FED2 was antibiosis, and FED3 was parasitism. Based on their morphological characteristics, FEB2, FEB5 and FED3 were identified as Helicomyces spp.; FEB1 was a Rhizopus sp.; FED1 was a Mucor sp.; and FED2 was a species of Penicillium.


1989 ◽  
Vol 53 (7) ◽  
pp. 1829-1836 ◽  
Author(s):  
Naoto YOSHIDA ◽  
Takayuki FUKUSHIMA ◽  
Hideki SAITO ◽  
Makoto SHIMOSAKA ◽  
Mitsuo OKAZAKI

2021 ◽  
Vol 12 ◽  
Author(s):  
Xinrong Zhang ◽  
Zhenhua Zhang ◽  
Xiao-Lin Chen

Redox modification, a post-translational modification, has been demonstrated to be significant for many physiological pathways and biological processes in both eukaryotes and prokaryotes. However, little is known about the global profile of protein redox modification in fungi. To explore the roles of redox modification in the plant pathogenic fungi, a global thiol proteome survey was performed in the model fungal pathogen Magnaporthe oryzae. A total of 3713 redox modification sites from 1899 proteins were identified through a mix sample containing mycelia with or without oxidative stress, conidia, appressoria, and invasive hyphae of M. oryzae. The identified thiol-modified proteins were performed with protein domain, subcellular localization, functional classification, metabolic pathways, and protein–protein interaction network analyses, indicating that redox modification is associated with a wide range of biological and cellular functions. These results suggested that redox modification plays important roles in fungal growth, conidium formation, appressorium formation, as well as invasive growth. Interestingly, a large number of pathogenesis-related proteins were redox modification targets, suggesting the significant roles of redox modification in pathogenicity of M. oryzae. This work provides a global insight into the redox proteome of the pathogenic fungi, which built a groundwork and valuable resource for future studies of redox modification in fungi.


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