PXD033387 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Interactions between paralogous bacterial enhancer binding proteins enable metal-dependent regulation of alternative nitrogenases in Azotobacter vinelandii |
Description | All diazotrophic bacteria and archaea isolated so far utilise a nitrogenase enzyme containing molybdenum in the active site co-factor to fix atmospheric dinitrogen to ammonia. However, in addition to the Mo-dependent nitrogenase, some nitrogen-fixing prokaryotes also express genetically distinct alternative nitrogenase isoenzymes, namely the V-dependent and Fe-only nitrogenases respectively. Nitrogenase isoenzymes are expressed hierarchically according to metal availability and catalytic efficiency. In proteobacteria, this hierarchy is maintained via stringent transcriptional regulation of gene clusters by dedicated bacterial enhancer binding proteins (bEBPs). The model diazotroph Azotobacter vinelandii contains two paralogs of the vanadium nitrogenase activator VnfA (henceforth, VnfA1), designated VnfA2 and VnfA3, with unknown functions. Here we demonstrate that the VnfA1 and VnfA3 bEBPs bind to the same target promoters in the Azotobacter vinelandii genome and co-activate a subset of genes in the absence of V, including the structural genes for the Fe only nitrogenase. Co-activation is inhibited by the presence of V and is dependent on an accessory protein VnfZ that is co-expressed with VnfA3. Our studies uncover a plethora of interactions between bEBPs required for nitrogen fixation, revealing unprecedented potential for fine tuning expression of alternative nitrogenases in response to metal availability. |
HostingRepository | PRIDE |
AnnounceDate | 2022-06-23 |
AnnouncementXML | Submission_2022-06-23_07:48:31.444.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD033387 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Carlo de Oliveira Martins |
SpeciesList | scientific name: Azotobacter vinelandii DJ; NCBI TaxID: 322710; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Eclipse |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-04-23 15:27:33 | ID requested | |
⏵ 1 | 2022-06-23 07:48:31 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Azotobacter, alternative nitrogenases, Co-IP, LC-MSMS |
Contact List
Ray Dixon |
contact affiliation | Group Leader, Department of Molecular Microbiology |
contact email | Ray.Dixon@jic.ac.uk |
lab head | |
Carlo de Oliveira Martins |
contact affiliation | John Innes Centre |
contact email | Carlo.Martins@jic.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD033387
- Label: PRIDE project
- Name: Interactions between paralogous bacterial enhancer binding proteins enable metal-dependent regulation of alternative nitrogenases in Azotobacter vinelandii