PXD012320

PXD012320 is an original dataset announced via ProteomeXchange.

Title	Interactome of the Escherichia coli nitrate reductase respiratory complex, NarGHI, under various metabolic conditions
Description	Cellular respiration is a fundamental process undergone within energy-transducing membranes through the redox activity of multimeric protein assemblies, so-called respiratory complexes. In most cases, electron transport is ensured by lipophilic molecules, quinones, serving as electron shuttles. This redox activity is coupled to the net translocation of protons across the membrane thereby establishing an electrochemical gradient, the protonmotive force (pmf). Such a gradient powers the transport of molecules (such as proteins, ions or antibiotics) and ATP synthesis but was also shown to participate in protein localization in prokaryotes. Importantly, energy-transducing membranes show a high level of organization with heterogeneous distribution of respiratory complexes as observed across several bacterial lineages. Although electron transport in energy-transducing membranes is considered to be a kinetic process coupled to the diffusion of all reactants and in particular quinones, it is not clear to which extent subcellular distribution of respiratory complexes can have an influence on the overall kinetics. We previously evidenced polar clustering of nitrate reductase, NarGHI, an anaerobic respiratory complex in the gut bacterium Escherichia coli. Such spatial organization was shown to directly impact the electron flux of the associated respiratory chain. While dynamic localization of such complex plays an important role in controlling respiration, the mechanism by which it impacts the electron flux is not understood. Yet, under such conditions where nitrate is the sole terminal electron acceptor, functioning of the electron transport chain in enteric bacteria such as E. coli and Salmonella typhimurium is associated with the production of nitric oxide (NO) mainly resulting from the reduction of nitrite by nitrate reductase. As a consequence, both E. coli and S. typhimurium produce a multitude of enzymes controlling NO homeostasis, the primary source of nitrosative stress. Protein S-nitrosylation is a ubiquitous NO-dependent post-translational modification of cysteine that regulates protein structure and function. Recently, Seth et al demonstrated that, in absence of oxygen, NO oxidation is mainly catalyzed by the hybrid cluster protein Hcp allowing its further reaction with thiols of a broad spectrum of proteins. Among Hcp-dependent S-nitrosylated targets are the nitrate reductase complex, multiple metabolic enzymes and the transcription factor OxyR whose S-nitrosylation entails a distinct nitrosative stress regulon. Optimizing electron transport through clustering of nitrate reductase will lead to nitrite accumulation which may in turn be responsible for NO production. Here, the electron-donating respiratory complex, the formate dehydrogenase, FdnGHI was shown to cluster at the poles under nitrate respiring conditions. Its proximity with the nitrate reductase complex was confirmed by evaluating the interactome of the later under distinct metabolic conditions reported to impact its subcellular organization. All the identified partners were exclusively found when cells were grown under nitrate respiration. The proximity of two respiratory complexes provides mechanistic explanation on the importance of subcellular organization onto quinone pool turnover. Noteworthy is the identification of several components playing key roles in the protection against endogenous nitrosative stress.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:52:11.532.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Luc Camoin
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-01-14 05:53:52	ID requested
1	2019-10-07 08:00:53	announced
2	2019-10-25 06:03:08	announced	2019-10-25: Updated publication reference for PubMed record(s): 31641084.
⏵ 3	2024-10-22 04:52:19	announced	2024-10-22: Updated project metadata.

10.1128/mbio.01832-19;

Bulot S, Audebert S, Pieulle L, Seduk F, Baudelet E, Espinosa L, Pizay MC, Camoin L, Magalon A, Clustering as a Means To Control Nitrate Respiration Efficiency and Toxicity in Escherichia coli. mBio, 10(5):(2019) [pubmed]

curator keyword: Biological

submitter keyword: NarGHI,Escherichia coli, nitrate respiration, label-free, interactome

Camoin Luc
contact affiliation	Marseille Proteomics, CRCM, Inserm, CNRS
contact email	luc.camoin@inserm.fr
lab head
Luc Camoin
contact affiliation	Life Sciences
contact email	luc.camoin@inserm.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD012320
     1. Label: PRIDE project
     2. Name: Interactome of the Escherichia coli nitrate reductase respiratory complex, NarGHI, under various metabolic conditions