PXD032867
PXD032867 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Proteome-wide lysine acetylation profiling to investigate the involvement of histone deacetylase HDA5 in the salt stress response of Arabidopsis leaves |
Description | Post-translational modifications (PTMs) of proteins play important roles in the acclimation of plants to environmental stress. Lysine acetylation is a dynamic and reversible PTM, which can be removed by histone deacetylases. Here we investigated the role of lysine acetylation in the response of Arabidopsis leaves to one week of salt stress. A quantitative mass spectrometry analysis revealed an increase in lysine acetylation of several proteins from cytosol and plastids, which was accompanied by an altered HDAC activity in the salt-treated leaves. While activities of HDA14 and HDA15 were decreased upon salt stress, HDA5 showed a mild and HDA19 a strongly increased activity. Since HDA5 is a cytosolic-nuclear enzyme from the class II histone deacetylase family with yet unknown protein substrates, we performed a lysine acetylome analysis on hda5 mutants and characterized its substrate proteins. Next to histone H2B, the salt stress responsive transcription factor GT2L and the dehydration-related protein ERD7 were identified as HDA5 substrates. In addition, in protein-protein interaction studies HDA18 was discovered, among other interacting proteins, to work in a complex together with HDA5. Altogether this study revealed the substrate proteins of HDA5 and identified new lysine acetylation sites which are hyperacetylated upon salt stress. The identification of the specific histone deacetylase substrate proteins, apart from histones, will be important to unravel the acclimation response of Arabidopsis to salt stress and their role in plant physiology. |
HostingRepository | jPOST |
AnnounceDate | 2023-03-28 |
AnnouncementXML | Submission_2023-03-28_05:48:48.722.xml |
DigitalObjectIdentifier | |
ReviewLevel | Non peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Jürgen Eirich |
SpeciesList | scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702; |
ModificationList | S-carboxamidomethyl-L-cysteine; L-methionine sulfoxide; alpha-amino acetylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2022-03-29 02:25:39 | ID requested | |
⏵ 1 | 2023-03-28 05:48:49 | announced |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Arabidopsis thaliana, Acetylation, Post-Translational Modifications, Histone deacetylase |
Contact List
Iris Finkemeier | |
---|---|
lab head | |
Jürgen Eirich | |
contact affiliation | University of Münster - WWU - Institute for Biology and Biotechnology of Plants |
dataset submitter |
Full Dataset Link List
jPOST dataset URI |
Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.jpostdb.org/JPST001545/ |