Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon

@article{Blasco2004NitrateRO,
  title={Nitrate reductases of Escherichia coli: Sequence of the second nitrate reductase and comparison with that encoded by the narGHJI operon},
  author={Francis Blasco and Chantal Iobbi and Jeanine Ratouchniak and Violaine Bonnefoy and Marc Chippaux},
  journal={Molecular and General Genetics MGG},
  year={2004},
  volume={222},
  pages={104-111}
}
SummaryThe structural genes for NRZ, the second nitrate reductase of Escherichia coli, have been sequenced. They are organized in a transcription unit, narZYWV, encoding four subunits, NarZ, NarY, NarW and NarV. The transcription unit is homologous (73% identity) to the narGHJI operon which encodes the genes for NRA, the better characterized nitrate reductase of this organism. The level of homology between the corresponding polypeptides ranges from 69% for the NarW/NarJ pair to 86% for the NarV… 
Nitrate reductases inEscherichia coli
TLDR
The expression of both thenarGHJI operon and thenarK gene are positively regulated by two transacting factors Fnr and NarL-Phosphate, activated respectively by anaerobiosis and nitrate, while the physiological role of the constitutively expressed nitrate reductase Z remains to be defined.
The roles of the polytopic membrane proteins NarK, NarU and NirC in Escherichia coli K‐12: two nitrate and three nitrite transporters
TLDR
In contrast to NirC, which transports only nitrite, NarK and NarU provide alternative mechanisms for both nitrate and nitrite transport, however, NarU might selectively promote nitrite ex‐cretion, not nitrite uptake.
Role of the Escherichia coli nitrate transport protein, NarU, in survival during severe nutrient starvation and slow growth.
TLDR
The data suggest that NarU confers a selective advantage during severe nutrient starvation or slow growth, conditions similar to those encountered in vivo.
Close genetic relationship between Nitrobacter hamburgensis nitrite oxidoreductase and Escherichia coli nitrate reductases
TLDR
The nitrite oxidoreductase (NOR) from the facultative nitrite-oxidizing bacterium Nitrobacter hamburgensis X14 was investigated genetically and the N-terminal amino acid sequence of the NOR β-subunit (NorB) was determined and an oligo-nucleotide was derived that was used for the identification and cloning of gene norB.
Two domains of a dual‐function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus
TLDR
Analysis of both the accumulation of intracellular nitrite and electron transport through the nitrate reductase enzyme in narK mutants reveals that NarK1 and NarK2 are both involved in nitrate uptake, indicating that narK2 encodes a nitrate/nitrite antiporter.
A nitrate reductase gene of the cyanobacterium Synechococcus PCC6301 inferred by heterologous hybridization, cloning and targeted mutagenesis
TLDR
Data suggest that pDN1 might encode a polypeptide of nitrate reductase, which is distinct from three clones of genes involved in nitrate assimilation that were isolated previously from the related cyanobacterium Synechococcus PCC7942.
The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA.
TLDR
The combined data indicate that NapF plays one or more currently unidentified roles in the post-translational modification of NapA prior to the export of folded NapA via the twin-arginine translocation pathway into the periplasm.
The Membrane‐Bound Nitrate Reductase A from Escherichia Coli: NarGHI
TLDR
The present article focuses on the advances obtained on NarGHI, its function and architecture, and the eight redox cofactors that form like an electrical wire through all the enzymes, starting from the electron acceptor site to the catalytic center.
Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone
TLDR
It is shown that the isolated twin‐arginine signal peptide of NapA is structured in its unbound form and undergoes a small but significant conformational change upon interaction with NapD, and points towards a role for NapD in the insertion of the molybdenum cofactor.
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