PXD041127 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | NirP1 is a small protein that controls nitrite-to-ammonium reduction in cyanobacteria |
Description | Unlike all other bacteria, the physiology of cyanobacteria is based on the assimilation of organic matter from inorganic carbon driven by oxygenic photosynthesis. This setting poses special regulatory challenges, particularly in integrating carbon and nitrogen metabolism. Several regulatory factors control the primary nitrogen metabolism, such as the PII protein and proteins interacting with it (PirA, PirC or PipX), or the inactivating factors IF7 and IF17 impacting glutamine synthetase activity. However, regulatory proteins of other enzymes in the nitrogen assimilation pathway have not been described thus far. Here, we show that the 81 amino acids regulatory protein NirP1 in the cyanobacterium Synechocystis sp. PCC 6803 functions as an inhibitor of nitrite reductase, a central enzyme in the assimilation of ammonia from nitrate/nitrite. Ectopic overexpression of the nirP1 gene under standard growth conditions led to a pigmentation phenotype and delayed growth, which was correlated by the excretion of nitrite and dramatic changes in metabolite pools. We show that nitrite excretion occurs in Synechocystis wild type cells upon the shift from high CO2 (HC) to low CO2 (LC) conditions when NirP1 expression becomes activated. The expression of nirP1 is controlled by two transcription factors, NtcA, which binds to a recognition site in a repressive position above the transcription start site (TSS), and an activator, which probably binds to an element 60 to 43 nt upstream of the TSS. Therefore, the joint activity of NtcA and this activator leads to the observed induction of NirP1 under LC conditions, whereas it is repressed by shifts to nitrogen starvation. The data demonstrate that NirP1 plays a crucial role in the coordination of C and N primary metabolism in cyanobacteria by targeting the activity of one of the central enzymes. In natural environments, the excreted nitrite will be utilized by other microorganisms; therefore, NirP1 will ultimately impact the activities and composition of the surrounding microbiome. |
HostingRepository | PRIDE |
AnnounceDate | 2024-02-23 |
AnnouncementXML | Submission_2024-02-23_06:54:55.674.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Philipp Spaet |
SpeciesList | scientific name: Synechocystis sp. PCC 6803; NCBI TaxID: 1148; scientific name: Bacteria; NCBI TaxID: NCBITaxon:2; |
ModificationList | No PTMs are included in the dataset |
Instrument | Orbitrap Exploris 480 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-03-27 04:07:55 | ID requested | |
⏵ 1 | 2024-02-23 06:54:56 | announced | |
Publication List
Keyword List
submitter keyword: photosynthesis,cyanobacteria, nitrogen assimilation, Synechocystis sp. PCC 6803, small proteins, gene expression, nitrite reductase, stress acclimation |
Contact List
Prof. Wolfgang R. Hess |
contact affiliation | Genetics and Experimental Bioinformatics, Faculty of Biology, Freiburg University, D-79104 Freiburg, Germany |
contact email | wolfgang.hess@biologie.uni-freiburg.de |
lab head | |
Philipp Spaet |
contact affiliation | University Tuebingen Department of Quantitative Proteomics |
contact email | philipp.spaet@uni-tuebingen.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD041127
- Label: PRIDE project
- Name: NirP1 is a small protein that controls nitrite-to-ammonium reduction in cyanobacteria