Proteomics

Dataset Information

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Tandem mass tags (TMT)–based quantitative proteomics approach quantified in 2-hydroxyisobutyrylation site of rice spikelets and Ustilaginoidea virens by mass spectrometry.


ABSTRACT: Rice false smut, caused by the pathogenic ascomycete fungus Ustilaginoidea virens (teleomorph: Villosiclava virens), is one of the most devastating grain diseases in the majority of rice-growing areas of the world. Lysine 2-hydroxyisobutyrylation (Khib) is a novel post-translational modification (PTM), which plays an important role in active gene transcription and cellular proliferation in eukaryotes. However, its function remains unknown in phytopathogens and plant. Here, we report a comprehensive identification of Khib in rice false smut fungus Ustilaginoidea virens and rice. By using a tandem mass tags (TMT)–based quantitative proteomics approach, 2-hydroxyisobutyrylation sites were identified in U. virens and rice.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Ustilaginoidea Virens Oryza Sativa (rice)

TISSUE(S): Whole Body

SUBMITTER: Xiaoyang Chen  

LAB HEAD: Lu zheng

PROVIDER: PXD019114 | Pride | 2023-06-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Z8428TP2o.raw Raw
Z8428TP2o_txt.zip Other
Z8428TQ_01.raw Raw
Z8428TQ_02.raw Raw
Z8428TQ_03.raw Raw
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Publications

Comprehensive identification of lysine 2-hydroxyisobutyrylated proteins in Ustilaginoidea virens reveals the involvement of lysine 2-hydroxyisobutyrylation in fungal virulence.

Chen Xiaoyang X   Li Xiabing X   Li Pingping P   Chen Xiaolin X   Liu Hao H   Huang Junbin J   Luo Chaoxi C   Hsiang Tom T   Zheng Lu L  

Journal of integrative plant biology 20210201 2


Lysine 2-hydroxyisobutyrylation (K<sub>hib</sub> ) is a newly identified post-translational modification (PTM) that plays important roles in transcription and cell proliferation in eukaryotes. However, its function remains unknown in phytopathogenic fungi. Here, we performed a comprehensive assessment of K<sub>hib</sub> in the rice false smut fungus Ustilaginoidea virens, using Tandem Mass Tag (TMT)-based quantitative proteomics approach. A total of 3 426 K<sub>hib</sub> sites were identified in  ...[more]

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