PXD013607

PXD013607 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2019-04-23 06:30:14	ID requested
⏵ 1	2019-12-09 02:34:31	announced

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]

curator keyword: Biological

submitter keyword: Bacillus subtilis/ allicin/ diallyl polysulfane/ bacillithiol/ S-thioallylation

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

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PRIDE project URI

• PRIDE
  1. PXD013607
     1. Label: PRIDE project
     2. Name: The sulfur stress response and protein S-thioallylation caused by allicin and diallyl polysulfanes in Bacillus subtilis as revealed by transcriptomics and proteomics