Proteomics

Dataset Information

0

Lysine 2-hydroxyisobutyrylatome profiling reveals extensive lysine 2-hydroxyisobutyrylation in common wheat

ABSTRACT: In this work, we first analyzed wheat (Triticum aestivum L.) lysine Khib sites by mass spectrometry. A total of 3,348 lysine modification sites from 1,047 proteins were identified in wheat seedlings. The identified Kcr proteins were discovered to be widespread. Bioinformatic data indicated these Kcr proteins involved in diverse biology and metabolic processes. Our data indicated that Khib is as dynamic as Kac and Khib changes in response to the deacetylase inhibitors Trichostatin A (TSA) and nicotinamide (NAM). We tested histone Khib and deacylation activities of several wheat HATs and HDACs using wheat Krnose EMS mutants. Finally, we confirmed lysine Khib on K206 of PGK was a regulatory modification using mustagenesis experiments and found that de-Khib impaired protein interactions of PGK. Our data demonstrate that the regulatory scope of lysine Khib is broad and comparable with that of other major PTMs. Wheat histone Khib are dynamically regulated by environmental cues and are likely to be removed by different mechanisms.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Triticum Aestivum (wheat)

TISSUE(S): Leaf

SUBMITTER: xiaomei li  

LAB HEAD: Feng Chen

PROVIDER: PXD012666 | Pride | 2022-12-31

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
Z8131PI2o.raw Raw
txt.zip Other
Items per page:
1 - 2 of 2
altmetric image

Publications

Global Profiling of 2-hydroxyisobutyrylome in Common Wheat.

Zhang Ning N   Zhang Lingran L   Li Linjie L   Geng Junyou J   Zhao Lei L   Ren Yan Y   Dong Zhongdong Z   Chen Feng F  

Genomics, proteomics & bioinformatics 20210211 4

As a novel post-translational modification (PTM), lysine 2-hydroxyisobutyrylation (Khib) is considered to regulate gene transcriptional activities in eukaryotic cells; however, the functions of Khib-modified proteins in plants remain unknown. Here, we report that Khib is an evolutionarily-conserved PTM in wheat and its progenitors. A total of 3348 Khib sites on 1074 proteins are identified in common wheat (Triticum aestivum L.) by using affinity purification and mass spectroscopy of 2-hydroxyiso  ...[more]

Similar Datasets

Proteomics Crotonylome profiling reveals extensive lysine crotonylation in common wheat
2023-07-20 | PXD008483 | Pride
Proteomics GlobaGlobal involvement of lysine crotonylation in protein modification and transcription regulation in ricel involvement of lysine crotonylation in protein modification and transcription regulation in rice
2018-07-23 | PXD008716 | Pride
Proteomics First comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts
2021-12-30 | PXD026445 | Pride
Proteomics Global Proteomic Analysis of Lysine crotonylation in The Plant Pathogen Botrytis cinerea
2020-09-07 | PXD019358 | Pride
Proteomics Global involvement of lysine crotonylation in protein modification and transcription regulation in rice
2018-09-20 | PXD010376 | Pride
Proteomics Global crotonylatome and function analysis of lysine-crotonylated proteins in wheat response to cold stress
2023-07-20 | PXD030768 | Pride
Proteomics Global analysis of lysine 2-hydroxyisobutyrylation in wheat root
2021-09-09 | PXD020819 | Pride
Proteomics Global analysis of lysine 2-hydroxyisobutyrylation in Rheum palmatum
2021-03-29 | PXD024730 | Pride
Proteomics Global analysis of lysine 2-hydroxyisobutyrylation in wheat leaf
2021-06-08 | PXD020788 | Pride
Proteomics Proteome analysis of lysine 2-hydroxyisobutyrylation in the peripheral blood of systemic lupus erythematosus patients
2023-03-10 | PXD015351 | Pride