PXD013607 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The sulfur stress response and protein S-thioallylation caused by allicin and diallyl polysulfanes in Bacillus subtilis as revealed by transcriptomics and proteomics |
Description | In this study, we compared the transcriptome signatures under allicin and diallyl tetrasulfane (DAS4) exposure in the Gram-positive bacterium B. subtilis. We further used shotgun proteomics to unravel the overall S-thioallylomes provoked by allicin and DAS4. Allicin and DAS4 caused a similar thiol-specific oxidative and electrophile stress response, protein and DNA damage in the transcriptome. At the proteome level, we identified in total 108 S-thioallylated proteins under allicin and/or DAS4 stress, while allicin appeared to have a stronger thiolation affect on redox-sensitive proteins. The S-thioallylome includes enzymes involved in the biosynthesis of surfactin (SrfAA, SrfAB), amino acids (SerA, MetE, YxjG, YitJ, CysJ, GlnA, YwaA), nucleotides (PurB, PurC, PyrAB, GuaB), translation factors (EF-Tu, EF-Ts, EF-G), antioxidant enzymes (AhpC, MsrB) as well as redox-sensitive MarR/OhrR and DUF24-family regulators (OhrR, HypR, YodB, CatR). Growth phenotype analysis revealed that the LMW thiol bacillithiol, the thiol-redox regulator Spx as well as the HypR and OhrR regulons confer protection against allicin and DAS4 stress. Altogether, we could show here that allicin and DAS4 cause both an oxidative and sulfur stress response in the transcriptome and widespread S-thioallylation of redox-sensitive proteins in B. subtilis. |
HostingRepository | PRIDE |
AnnounceDate | 2019-12-09 |
AnnouncementXML | Submission_2019-12-09_02:34:30.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Van Loi Vu |
SpeciesList | scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308; |
ModificationList | N-ethylmaleimide derivatized cysteine; L-methionine (S)-sulfoxide |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-04-23 06:30:14 | ID requested | |
⏵ 1 | 2019-12-09 02:34:31 | announced | |
Publication List
Chi BK, Huyen NTT, Loi VV, Gruhlke MCH, Schaffer M, M, ä, der U, Maa, ß S, Becher D, Bernhardt J, Arbach M, Hamilton CJ, Slusarenko AJ, Antelmann H, as Revealed by Transcriptomics and Proteomics. Antioxidants (Basel), 8(12):(2019) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Bacillus subtilis/ allicin/ diallyl polysulfane/ bacillithiol/ S-thioallylation |
Contact List
Prof. Dr. Haike Antelmann |
contact affiliation | Freie Universität Berlin Institut für Biologie-Mikrobiologie |
contact email | haike.antelmann@fu-berlin.de |
lab head | |
Van Loi Vu |
contact affiliation | Freie Universität Berlin |
contact email | vu.v.loi@fu-berlin.de |
dataset submitter | |
Full Dataset Link List
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.pride.ebi.ac.uk/pride/data/archive/2019/12/PXD013607 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD013607
- Label: PRIDE project
- Name: The sulfur stress response and protein S-thioallylation caused by allicin and diallyl polysulfanes in Bacillus subtilis as revealed by transcriptomics and proteomics