PXD012537

PXD012537 is an original dataset announced via ProteomeXchange.

Title	Proteomic analysis of lysine acetylation provides strong evidence for involvement of acetylated histone and chloroplast proteins in CWMV infected plant
Description	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.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:21:44.924.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	xiaonan fu
SpeciesList	scientific name: Nicotiana tabacum (Common tobacco); NCBI TaxID: 4097;
ModificationList	acetylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2019-01-28 06:56:53	ID requested
1	2021-05-06 23:16:50	announced
⏵ 2	2024-10-22 05:21:45	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

curator keyword: Biological

submitter keyword: lysine acetylation,CWMV, photosynthesis, histone H3, chloroplast

Jianping Chen
contact affiliation	Institute of Plant Virology, Ningbo University, Ningbo, China
contact email	jpchen2001@126.com
lab head
xiaonan fu
contact affiliation	zhejiang scientific technology universitiy
contact email	2016460649@qq.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012537
     1. Label: PRIDE project
     2. Name: Proteomic analysis of lysine acetylation provides strong evidence for involvement of acetylated histone and chloroplast proteins in CWMV infected plant