PXD037804 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Physiology of trans-translation deficiency in Bacillus subtilis – a comparative proteomics study |
Description | trans-Translation is the most effective ribosome rescue system known in bacteria. While it is essential in some bacteria, Bacillus subtilis possesses two additional alternative ribosome rescue mechanisms that require the proteins BrfA or RqcH. To investigate the physiology of trans-translation deficiency in the model organism B. subtilis, we compared the proteomes of B. subtilis 168 and a ΔssrA mutant in mid-log phase using gel-free label-free quantitative proteomics. |
HostingRepository | PRIDE |
AnnounceDate | 2023-06-30 |
AnnouncementXML | Submission_2023-06-30_08:34:36.462.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | MelissaVázquez-Hernández |
SpeciesList | scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308; |
ModificationList | No PTMs are included in the dataset |
Instrument | Synapt MS |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-10-28 07:26:14 | ID requested | |
⏵ 1 | 2023-06-30 08:34:36 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: LC-MSE,translation, gene regulation, bacteria, proteome |
Contact List
Julia E.Bandow |
contact affiliation | Applied Microbiology, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44892 Bochum, Germany |
contact email | julia.bandow@rub.de |
lab head | |
MelissaVázquez-Hernández |
contact affiliation | Ruhr University Bochum |
contact email | melissa.vazquez-hernandez@rub.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD037804
- Label: PRIDE project
- Name: Physiology of trans-translation deficiency in Bacillus subtilis – a comparative proteomics study