Proteomic analysis of lysine acetylation provides strong evidence for involvement of acetylated histone and chloroplast proteins in CWMV infected plant

ABSTRACT: Protein lysine acetylation (Kac) is an important post-translational modification (PTM) mechanism in both eukaryotes and prokaryotes, with key roles in cellular regulation. To investigate the role of Kac in plants infected with virus, we characterized the lysine acetylome of Nicotiana benthamiana plants with or without a Chinese Wheat Mosaic Virus (CWMV) infection by using TMT labeling-based protein modification differential analysis, high-resolution liquid chromatography mass spectrometry analysis, and integrated bioinformatics analysis. Here, we identified 4803 acetylated lysine sites on 1964 proteins. A comparison of the acetylation levels of the CWMV-infected group with those of the uninfected group revealed that 747 sites were up-regulated on 422 proteins, including chloroplast localization proteins and histone H3, and 150 sites were down-regulated on 102 proteins when using a change threshold of at least 1.2 times and a t-test p-value of <0.05. Nineteen conserved motifs were extracted; 51% of the identified proteins were localized to the chloroplast. Among the acetylated proteins, 19 Kac sites were combined in core histones, including 10 Kac sites on histone 3. Bioinformatics analysis revealed that Kac occurs on a diverse range of proteins involved in a wide variety of biological processes, especially photosynthesis. Furthermore, we demonstrate that the acetylation level of chloroplast localization proteins and histone H3 are significantly increased. In summary, our results reveal the regulatory roles of Kac in response to CWMV infection.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Nicotiana Tabacum (common Tobacco)

TISSUE(S): Leaf

SUBMITTER: xiaonan fu  

LAB HEAD: Jianping Chen

PROVIDER: PXD012537 | Pride | 2021-05-07

REPOSITORIES: Pride