PXD006121 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis |
Description | DNA processing chain A (DprA) is a DNA binding protein which is ubiquitous in bacteria and required for DNA transformation. However, the interaction of DprA with competence proteins and recombination is poorly understood. Therefore, the proteomes of whole Neisseria meningitidis (Nm) wildtype and dprA mutant cells were compared. Such a comparative proteomic analysis increases our understanding of the interactions of DprA with other Nm components, and may elucidate its potential role beyond DNA processing in transformation. Using label-free quantitative proteomics, a total of 1057 unique Nm proteins were identified out of which 100 were quantified as differentially abundant (P ≤ 0.05 and fold change ≥ |2|) in the dprA null mutant. Proteins involved in homologous recombination (RecA, UvrD and HolA), pilus biogenesis (PilG, PilT1, PilT2, PilM, PilO, PilQ, PilF and PilE), and cell division, including core energy metabolism and response to oxidative stress were downregulated in dprA null mutant Nm. Immunoblotting was employed to validate the differences observed in two selected proteins. The analysis revealed reduced amounts of PilG in the dprA null mutant and reduced amounts of DprA in the Nm pilG null mutant. In conclusion, DprA interacts with proteins essential for Nm DNA recombination in transformation, pilus biogenesis and other functions associated with the inner membrane. Inverse downregulation of Nm DprA and PilG expression in the corresponding mutants indicate a link between DNA processing and pilus biogenesis demonstrated for the first time. |
HostingRepository | PRIDE |
AnnounceDate | 2017-04-26 |
AnnouncementXML | Submission_2017-04-26_05:10:52.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Shewit Kalayou |
SpeciesList | scientific name: Neisseria meningitidis serogroup B; NCBI TaxID: 491; |
ModificationList | monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-03-20 04:50:02 | ID requested | |
⏵ 1 | 2017-04-26 05:10:57 | announced | |
Publication List
Beyene GT, Kalayou S, Riaz T, Tonjum T, Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis. BMC Microbiol, 17(1):96(2017) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: Neisseria meningitides, DNA processing, pilus biogenesis, DprA, PilG, proteomics, mass spectrometry |
Contact List
Prof Tone Tønjum |
contact affiliation | Department of Microbiology, Institute of Clinical medicine, University of Oslo, Norway. |
contact email | tone.tonjum@medisin.uio.no |
lab head | |
Shewit Kalayou |
contact affiliation | Genome dynamics group, Oslo University Hospital |
contact email | shetek@rr-research.no |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD006121
- Label: PRIDE project
- Name: Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis