The Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
AuthorsBorrero-de Acuña, José Manuel
Timmis, Kenneth N
MetadataShow full item record
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.
CitationThe Protein Network of the Pseudomonas aeruginosa Denitrification Apparatus. 2016: J. Bacteriol.
AffiliationHelmholtz Centre for infection research (HZI), Inhoffenstraße 7, 38124 Braunschweig, Germany.
JournalJournal of bacteriology
The following license files are associated with this item:
- Protein complex formation during denitrification by Pseudomonas aeruginosa.
- Authors: Borrero-de Acuña JM, Timmis KN, Jahn M, Jahn D
- Issue date: 2017 Nov
- A Periplasmic Complex of the Nitrite Reductase NirS, the Chaperone DnaK, and the Flagellum Protein FliC Is Essential for Flagellum Assembly and Motility in Pseudomonas aeruginosa.
- Authors: Borrero-de Acuña JM, Molinari G, Rohde M, Dammeyer T, Wissing J, Jänsch L, Arias S, Jahn M, Schobert M, Timmis KN, Jahn D
- Issue date: 2015 Oct
- Nitric oxide signaling and transcriptional control of denitrification genes in Pseudomonas stutzeri.
- Authors: Vollack KU, Zumft WG
- Issue date: 2001 Apr
- Localization of denitrification genes on the chromosomal map of Pseudomonas aeruginosa.
- Authors: Vollack KU, Xie J, Härtig E, Römling U, Zumft WG
- Issue date: 1998 Feb
- The nitrate-sensing NasST system regulates nitrous oxide reductase and periplasmic nitrate reductase in Bradyrhizobium japonicum.
- Authors: Sánchez C, Itakura M, Okubo T, Matsumoto T, Yoshikawa H, Gotoh A, Hidaka M, Uchida T, Minamisawa K
- Issue date: 2014 Oct