Nitrate respiration in the actinomycete Streptomyces coelicolor

2005 ◽  
Vol 33 (1) ◽  
pp. 210-212 ◽  
Author(s):  
G. van Keulen ◽  
J. Alderson ◽  
J. White ◽  
R.G. Sawers
Keyword(s):  
Nitrate Reductase ◽  
Streptomyces Coelicolor ◽  
Nitrate Respiration ◽  
Obligate Aerobic ◽  
Respiratory Nitrate Reductase ◽  
Nitrate Reductases

Streptomyces coelicolor is an obligate aerobic, filamentous soil-dwelling bacterium. Remarkably, the genome of S. coelicolor has three copies of the narGHJI operon that encodes respiratory nitrate reductase. This review summarizes our current views on the requirements for multiple nitrate reductases in S. coelicolor.

scholarly journals Activity of Spore-Specific Respiratory Nitrate Reductase 1 ofStreptomyces coelicolorA3(2) Requires a Functional Cytochromebcc-aa3Oxidase Supercomplex

2019 ◽  
Vol 201 (11) ◽  
Author(s):  
Dörte Falke ◽  
Bianca Biefel ◽  
Alexander Haase ◽  
Stefan Franke ◽  
Marco Fischer ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Nitrate Reductase ◽  
Nitrate Reduction ◽  
Streptomyces Coelicolor ◽  
Nitrate Respiration ◽  
Nitrate Transport ◽  
Developmental Cycle ◽  
Content Type ◽  
Resting Spores ◽  
Respiratory Nitrate Reductase

ABSTRACTSpores have strongly reduced metabolic activity and are produced during the complex developmental cycle of the actinobacteriumStreptomyces coelicolor. Resting spores can remain viable for decades, yet little is known about how they conserve energy. It is known, however, that they can reduce either oxygen or nitrate using endogenous electron sources.S. coelicoloruses either a cytochromebdoxidase or a cytochromebcc-aa3oxidase supercomplex to reduce oxygen, while nitrate is reduced by Nar-type nitrate reductases, which typically oxidize quinol directly. Here, we show that in resting spores the Nar1 nitrate reductase requires a functionalbcc-aa3supercomplex to reduce nitrate. Mutants lacking the completeqcr-ctagenetic locus encoding thebcc-aa3supercomplex showed no Nar1-dependent nitrate reduction. Recovery of Nar1 activity was achieved by genetic complementation but only when the completeqcr-ctalocus was reintroduced to the mutant strain. We could exclude that the dependence on the supercomplex for nitrate reduction was via regulation of nitrate transport. Moreover, the catalytic subunit, NarG1, of Nar1 was synthesized in theqcr-ctamutant, ruling out transcriptional control. Constitutive synthesis of Nar1 in mycelium revealed that the enzyme was poorly active in this compartment, suggesting that the Nar1 enzyme cannot act as a typical quinol oxidase. Notably, nitrate reduction by the Nar2 enzyme, which is active in growing mycelium, was not wholly dependent on thebcc-aa3supercomplex for activity. Together, our data suggest that Nar1 functions together with the proton-translocatingbcc-aa3supercomplex to increase the efficiency of energy conservation in resting spores.IMPORTANCEStreptomyces coelicolorforms spores that respire with either oxygen or nitrate, using only endogenous electron donors. This helps maintain a membrane potential and, thus, viability. Respiratory nitrate reductase (Nar) usually receives electrons directly from reduced quinone species; however, we show that nitrate respiration in spores requires a respiratory supercomplex comprising cytochromebccoxidoreductase andaa3oxidase. Our findings suggest that the Nar1 enzyme in theS. coelicolorspore functions together with the proton-translocatingbcc-aa3supercomplex to help maintain the membrane potential more efficiently. Dissecting the mechanisms underlying this survival strategy is important for our general understanding of bacterial persistence during infection processes and of how bacteria might deal with nutrient limitation in the natural environment.

scholarly journals Hypoxia-induced synthesis of respiratory nitrate reductase 2 of Streptomyces coelicolor A3(2) depends on the histidine kinase OsdK in mycelium but not in spores

Microbiology ◽  
2019 ◽  
Vol 165 (8) ◽  
pp. 905-916 ◽  
Author(s):  
Marco Fischer ◽  
Dörte Falke ◽  
Jakob Rönitz ◽  
Alexander Haase ◽  
Timon Damelang ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Histidine Kinase ◽  
Streptomyces Coelicolor ◽  
Respiratory Nitrate Reductase

Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient in nitrate respiration

1997 ◽  
Vol 167 (1) ◽  
pp. 61-66 ◽  
Author(s):  
Heather J. Sears ◽  
Phillip J. Little ◽  
D. J. Richardson ◽  
B. C. Berks ◽  
Stephen Spiro ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Paracoccus Denitrificans ◽  
Nitrate Respiration

scholarly journals Two Nitrate/Nitrite Transporters Are Encoded within the Mobilizable Plasmid for Nitrate Respiration of Thermus thermophilus HB8

2000 ◽  
Vol 182 (8) ◽  
pp. 2179-2183 ◽  
Author(s):  
Sandra Ramírez ◽  
Renata Moreno ◽  
Olga Zafra ◽  
Pablo Castán ◽  
Cristina Vallés ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Average Distance ◽  
Thermus Thermophilus ◽  
Major Facilitator Superfamily ◽  
Nitrate Respiration ◽  
Mobilizable Plasmid ◽  
Excretion Rates ◽  
Major Facilitator ◽  
Nitrate And Nitrite

ABSTRACT Thermus thermophilus HB8 can grow anaerobically by using a membrane-bound nitrate reductase to catalyze the reduction of nitrate as a final electron acceptor in respiration. In contrast to other denitrifiers, the nitrite produced does not continue the reduction pathway but accumulates in the growth medium after its active extrusion from the cell. We describe the presence of two genes,narK1 and narK2, downstream of the nitrate reductase-encoding gene cluster (nar) that code for two homologues to the major facilitator superfamily of transporters. The sequences of NarK1 and NarK2 are 30% identical to each other, but whereas NarK1 clusters in an average-distance tree with putative nitrate transporters, NarK2 does so with putative nitrite exporters. To analyze whether this differential clustering was actually related to functional differences, we isolated derivatives with mutations of one or both genes. Analysis revealed that single mutations had minor effects on growth by nitrate respiration, whereas a double narK1 narK2 mutation abolished this capability. Further analysis allowed us to confirm that the double mutant is completely unable to excrete nitrite, while single mutants have a limitation in the excretion rates compared with the wild type. These data allow us to propose that both proteins are implicated in the transport of nitrate and nitrite, probably acting as nitrate/nitrite antiporters. The possible differential roles of these proteins in vivo are discussed.

scholarly journals Periplasmic nitrate reduction in Wolinella succinogenes: cytoplasmic NapF facilitates NapA maturation and requires the menaquinol dehydrogenase NapH for membrane attachment

Microbiology ◽  
2009 ◽  
Vol 155 (8) ◽  
pp. 2784-2794 ◽  
Author(s):  
Melanie Kern ◽  
Jörg Simon
Keyword(s):  
Electron Transport ◽  
Nitrate Reductase ◽  
Deletion Mutant ◽  
Electron Flow ◽  
Gene Clusters ◽  
Nitrate Respiration ◽  
Wolinella Succinogenes ◽  
Periplasmic Nitrate Reductase ◽  
Iron Sulfur ◽  
Membrane Bound

Various nitrate-reducing bacteria produce proteins of the periplasmic nitrate reductase (Nap) system to catalyse electron transport from the membraneous quinol pool to the periplasmic nitrate reductase NapA. The composition of the corresponding nap gene clusters varies but, in addition to napA, genes encoding at least one membrane-bound quinol dehydrogenase module (NapC and/or NapGH) are regularly present. Moreover, some nap loci predict accessory proteins such as the iron–sulfur protein NapF, whose function is poorly understood. Here, the role of NapF in nitrate respiration of the Epsilonproteobacterium Wolinella succinogenes was examined. Immunoblot analysis showed that NapF is located in the membrane fraction in nitrate-grown wild-type cells whereas it was found to be a soluble cytoplasmic protein in a napH deletion mutant. This finding indicates the formation of a membrane-bound NapGHF complex that is likely to catalyse NapH-dependent menaquinol oxidation and electron transport to the iron–sulfur adaptor proteins NapG and NapF, which are located on the periplasmic and cytoplasmic side of the membrane, respectively. The cysteine residues of a CX3CP motif and of the C-terminal tetra-cysteine cluster of NapH were found to be required for interaction with NapF. A napF deletion mutant accumulated the catalytically inactive cytoplasmic NapA precursor, suggesting that electron flow or direct interaction between NapF and NapA facilitated NapA assembly and/or export. On the other hand, NapA maturation and activity was not impaired in the absence of NapH, demonstrating that soluble NapF is functional. Each of the four tetra-cysteine motifs of NapF was modified but only one motif was found to be essential for efficient NapA maturation. It is concluded that the NapGHF complex plays a multifunctional role in menaquinol oxidation, electron transfer to periplasmic NapA and maturation of the cytoplasmic NapA precursor.

RNA-seq analyses reveal insights into the function of respiratory nitrate reductase of the diazotroph Herbaspirillum seropedicae

2016 ◽  
Vol 18 (8) ◽  
pp. 2677-2688 ◽  
Author(s):  
Paloma Bonato ◽  
Marcelo B. Batista ◽  
Doumit Camilios-Neto ◽  
Vânia C. S. Pankievicz ◽  
Michelle Z. Tadra-Sfeir ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Rna Seq ◽  
Herbaspirillum Seropedicae ◽  
Respiratory Nitrate Reductase
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