Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.7.1.2 (nitrate reductase)
 3,861 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The herbicide chlorate has been used extensively to isolate mutants that are defective in nitrate reduction. Chlorate is a substrate for the enzyme nitrate reductase (NR), which reduces chlorate to the toxic chlorite. Because NR is a substrate (NO(3) (-))-inducible enzyme, we investigated the possibility that chlorate may also act as an inducer. Irrigation of ammonia-grown Arabidopsis plants with chlorate leads to an increase in NR mRNA in the leaves. No such increase was observed for nitrite reductase mRNA following chlorate treatment; thus, the effect seems to be specific to NR. The increase in NR mRNA did not depend on the presence of wild-type levels of NR activity or molybdenum-cofactor, as a molybdenum-cofactor mutant with low levels of NR activity displayed the same increase in NR mRNA following chlorate treatment. Even though NR mRNA levels were found to increase after chlorate treatment, no increase in NR protein was detected and the level of NR activity dropped. The lack of increase in NR protein was not due to inactivation of the cells' translational machinery, as pulse labeling experiments demonstrated that total protein synthesis was unaffected by the chlorate treatment during the time course of the experiment. Chlorate-treated plants still retain the capacity to make functional NR because NR activity could be restored by irrigating the chlorate-treated plants with nitrate. The low levels of NR protein and activity may be due to inactivation of NR by chlorite, leading to rapid degradation of the enzyme. Thus, chlorate treatment stimulates NR gene expression in Arabidopsis that is manifested only at the mRNA level and not at the protein or activity level.
 ...
PMID:Effect of Chlorate Treatment on Nitrate Reductase and Nitrite Reductase Gene Expression in Arabidopsis thaliana. 1666 25

The use of chlorate as a selective inhibitor of dissimilative nitrate reduction was studied using pure cultures of Comamonas testosteroni (a denitrifier) and Klebsiella pneumoniae (a nitrate-ammonifier) isolated from estuarine sediment, and in sediment slurry. Pure culture experiments demonstrated that chlorate selectively inhibited membrane-bound nitrate reductase (Nar) activity, probably by blocking nitrate transporters (NarK). Sediment slurry experiments showed that chlorate inhibited nitrate reduction and N(2)O formation, but did not inhibit nitrite reduction and its N(2)O formation, indicating that chlorate selectively inhibited only the first step of nitrate reduction. Chlorite chemically oxidized nitrite to nitrate and could not be used as a selective inhibitor of nitrite metabolism, although chlorite apparently selectively inhibited formation of N(2)O from nitrite. Chlorate can be used as a specific inhibitor to distinguish between nitrate reduction by Nap or Nar in natural communities of microorganisms.
 ...
PMID:Use of chlorate as a selective inhibitor to distinguish membrane-bound nitrate reductase (Nar) and periplasmic nitrate reductase (Nap) of dissimilative nitrate reducing bacteria in sediment. 1971 7

Previous research has suggested that nitrate-respiring pathogens such as Escherichia coli O157:H7 and Salmonella spp. are susceptible to chlorate salts due to the conversion of chlorate to chlorite by respiratory nitrate reductase. This study was conducted to determine the effect of chlorate on E. coli O157:H7 growth and chlorate biotransformation and to determine whether chlorite is produced in anaerobic culture of E. coli O157:H7. Final concentrations of E. coli O157:H7 were generally decreased by about 2 log units in incubations containing > or =5 mM chlorate, except when bacteria were pretreated with 10 mM chlorate. [(36)Cl]Chlorate metabolism by pure cultures of E. coli O157:H7 was not measurable above chlorate concentrations of 5 mM, but measurable chlorate reduction occurred in cultures containing 0.5, 1, or 5 mM [(36)Cl]chlorate. Pretreatment of E. coli O157:H7 with 5 mM nitrate did not increase the rate of chlorate conversion to chloride, suggesting that nitrate did not induce nitrate reductase isoforms capable of metabolizing chlorate in E. coli O157:H7. Pure cultures of E. coli O157:H7 preconditioned with 10 mM chlorate had an attenuated ability to transform [(36)Cl]chlorate to [(36)Cl]chloride with measurable chlorate reduction only occurring in 0.5 mM chlorate treatments. The hypothesis that E. coli O157:H7 is sensitive to chlorate by virtue of the reduction of chlorate to chlorite ion (ClO(2)(-)) was supported, but not proven, by the direct measurement of low concentrations of [(36)Cl]ClO(2)(-) in incubation media containing 0.5 mM [(36)Cl]ClO(3)(-). Collectively these results indicate that growth of E. coli O157:H7 in pure culture will be reduced in the presence of 5 mM or greater concentrations of sodium chlorate and that E. coli O157:H7 is capable of producing chlorite ions during the metabolism of chlorate.
 ...
PMID:Chlorate metabolism in pure cultures of Escherichia coli O157:H7 pretreated with either nitrate or chlorate. 1982 35

Biochemical and genetical characterization of a rice nitrate reductase (NR)-deficient mutant, M819, which had been isolated as a chlorate-resistant mutant, was carried out. In M819, leaf NADH-NR activity was found to be about 10% of that of the wild-type cv 'Norin 8', while NADPH-NR activity was higher than that in the wild-type; FMNH2-NR and MV-NR activities were also 10% of those of the wild type; BPB-NR activity was higher than that of the wild type; and xanthine dehydrogenase activity was revealed to be present in both. These results suggest that the mutant line M819 lacks the functional heme domain of the NADH-NR polypeptide due to a point mutation or a small deletion within the coding region of the structural gene. Chlorate resistance in M819 was transmitted by a single recessive nuclear gene.
...
PMID:Characterization of a rice (Oryza sativa L.) mutant deficient in the heme domain of nitrate reductase. 2420 21

Cell suspensions of diploid Arabidopsis thaliana were screened for resistance to chlorate on a medium with ammonium nitrate as the nitrogen source, and after plating on filters to increase the plating efficiency. Thirty-nine lines were selected, four of which were still resistant after two years of subculturing on non-selective medium. Of the latter lines three were nitrate reductase deficient but exhibited some residual nitrate reductase activity; the fourth line showed a high level of enzyme activity. Screening M2-seeds for callus production on selective medium with amino acids as the nitrogen source and chlorate revealed resistant calli in 17 out of 483 M2-groups. Nine well-growing lines, all but one (G3) exhibiting no detectable in vivo nitrate reductase activity, were classified as defective in the cofactor. Two lines (G1 and G3) could be analysed genetically at the plant level. Chlorate resistance was monogenic and recessive. Sucrose gradient fractionation of callus extracts of G1 revealed that a complete enzyme molecule can be assembled. Nitrate reductase activity in G1 could partly be restored by excess molybdenum. It is suggested that G1 is disturbed in the catalytic properties of the cofactor. It appeared that G1 is neither allelic with another molybdenum repairable mutant (B73) nor with another cofactor mutant (B25). Wilting of intact G1 plants could be ascribed to non-closing stomata.
...
PMID:Nitrate reductase deficient cell lines from diploid cell cultures and lethal mutant M2 plants of Arabidopsis thaliana. 2424 70

Chlorate resistant mutants of Arabidopsis thaliana were isolated, of which 10 exhibited a lowered nitrate reductase activity and 51 were chlorate-resistant because of an impaired uptake of chlorate. The 51 mutants of this type are all affected in the same gene. The mutants with a lowered nitrate reductase activity fall into 7 different complementation groups. Three of these mutants grow poorly on media with nitrate as the sole nitrogen source, while the others apparently can reduce sufficient nitrate to bring about growth. In all cases a low nitrate reductase activity coincides with an enhanced nitrite reductase activity. After sucrose gradient centrifugation of wildtype extracts nitrate reductase is found at the 8S position, whereas cytochrome-c reductase is found both at 4 and 8S positions. It is suggested that the functional nitrate reductase is a complex consisting of 4S subunits showing cytochrome-c reductase activity and a Mo-bearing cofactor. All mutants except B25 are capable of assembling the 4S subunits into complexes which for most mutants have a lower S value and exhibit a lower nitrate reductase activity than the wildtype complexes. Since the mutants B25 and B73 exhibit a low xanthine dehydrogenase activity, the Mo-bearing cofactor is probably less available in these mutants than in the wildtype. B73 appears to be the only mutant which is partly repaired by excessive Mo. The possible role of several genes is discussed.
...
PMID:Isolation and characterization of nitrate reductase-deficient mutants of Arabidopsis thaliana. 2426 29


<< Previous 1 2 3