2.50
Hdl Handle:
http://hdl.handle.net/10033/600935
Title:
The Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus.
Authors:
Borrero-de Acuña, José Manuel; Rohde, Manfred ( 0000-0003-0522-3580 ) ; Wissing, Josef; Jänsch, Lothar; Schobert, Max; Molinari, Gabriella ( 0000-0002-6781-1292 ) ; Timmis, Kenneth N; Jahn, Martina; Jahn, Dieter
Abstract:
Oxidative phosphorylation using multiple component, membrane-associated protein complexes is the most effective way for a cell to generate energy. Here, we systematically investigated the multiple protein-protein interactions of the denitrification apparatus of the pathogenic bacterium Pseudomonas aeruginosa. During denitrification, nitrate (Nar), nitrite (Nir), nitric-oxide (Nor) and nitrous-oxide (Nos) reductases catalyze the reaction cascade of NO(3-) → NO(2-) → NO → N2O → N2. Genetic experiments suggested that the nitric-oxide reductase NorBC and the regulatory protein NosR are the nucleus of the denitrification protein network. We utilized membrane interactomics in combination with electron microscopy co-localization studies to elucidate the corresponding protein-protein interactions. The integral membrane proteins NorC, NorB and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. The periplasmic nitrous-oxide reductase, NosZ, is linked via NosR. The nitrate transporter, NarK2, the nitrate regulatory system, NarXL, various nitrite reductase maturation proteins, NirEJMNQ, and the Nos assembly lipoproteins, NosFL, were also found to be attached. A number of proteins associated with energy generation, including electron donating dehydrogenases, the complete ATP synthase, almost all enzymes of the TCA cycle, and the SEC system of protein transport, among many other proteins, were found to interact with the denitrification proteins. This deduced nitrate respirasome is presumably only one part of an extensive cytoplasmic membrane-anchored protein network connecting cytoplasmic, inner membrane and periplasmic proteins, to mediate key activities occurring at the barrier/interface between the cytoplasm and the external environment.
Affiliation:
Helmholtz Centre for infection research (HZI), Inhoffenstraße 7, 38124 Braunschweig, Germany.
Citation:
The Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus. 2016: J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
22-Feb-2016
URI:
http://hdl.handle.net/10033/600935
DOI:
10.1128/JB.00055-16
PubMed ID:
26903416
Type:
Article
ISSN:
1098-5530
Appears in Collections:
publications of the central unit for microscopy (ZEIM)

Full metadata record

DC FieldValue Language
dc.contributor.authorBorrero-de Acuña, José Manuelen
dc.contributor.authorRohde, Manfreden
dc.contributor.authorWissing, Josefen
dc.contributor.authorJänsch, Lotharen
dc.contributor.authorSchobert, Maxen
dc.contributor.authorMolinari, Gabriellaen
dc.contributor.authorTimmis, Kenneth Nen
dc.contributor.authorJahn, Martinaen
dc.contributor.authorJahn, Dieteren
dc.date.accessioned2016-03-08T14:41:35Zen
dc.date.available2016-03-08T14:41:35Zen
dc.date.issued2016-02-22en
dc.identifier.citationThe Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus. 2016: J. Bacteriol.en
dc.identifier.issn1098-5530en
dc.identifier.pmid26903416en
dc.identifier.doi10.1128/JB.00055-16en
dc.identifier.urihttp://hdl.handle.net/10033/600935en
dc.description.abstractOxidative phosphorylation using multiple component, membrane-associated protein complexes is the most effective way for a cell to generate energy. Here, we systematically investigated the multiple protein-protein interactions of the denitrification apparatus of the pathogenic bacterium Pseudomonas aeruginosa. During denitrification, nitrate (Nar), nitrite (Nir), nitric-oxide (Nor) and nitrous-oxide (Nos) reductases catalyze the reaction cascade of NO(3-) → NO(2-) → NO → N2O → N2. Genetic experiments suggested that the nitric-oxide reductase NorBC and the regulatory protein NosR are the nucleus of the denitrification protein network. We utilized membrane interactomics in combination with electron microscopy co-localization studies to elucidate the corresponding protein-protein interactions. The integral membrane proteins NorC, NorB and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. The periplasmic nitrous-oxide reductase, NosZ, is linked via NosR. The nitrate transporter, NarK2, the nitrate regulatory system, NarXL, various nitrite reductase maturation proteins, NirEJMNQ, and the Nos assembly lipoproteins, NosFL, were also found to be attached. A number of proteins associated with energy generation, including electron donating dehydrogenases, the complete ATP synthase, almost all enzymes of the TCA cycle, and the SEC system of protein transport, among many other proteins, were found to interact with the denitrification proteins. This deduced nitrate respirasome is presumably only one part of an extensive cytoplasmic membrane-anchored protein network connecting cytoplasmic, inner membrane and periplasmic proteins, to mediate key activities occurring at the barrier/interface between the cytoplasm and the external environment.en
dc.languageENGen
dc.titleThe Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research (HZI), Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journalJournal of bacteriologyen

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.