Identification of the Arabidopsis CHL3 Gene as the Nitrate Reductase Structural Gene NIA2

1991 ◽  
Vol 3 (5) ◽  
pp. 461 ◽  
Author(s):  
Jack Q. Wilkinson ◽  
Nigel M. Crawford
Keyword(s):  
Nitrate Reductase ◽  
Structural Gene

Distinction of cnxH cofactor gene-specified protomers with monoclonal antibodies to Aspergillus nitrate reductase

1988 ◽  
Vol 34 (1) ◽  
pp. 68-72 ◽  
Author(s):  
R. J. Downey ◽  
P. A. South
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Nitrate Reductase ◽  
Aspergillus Nidulans ◽  
Structural Gene ◽  
Molybdenum Cofactor ◽  
Native Enzyme ◽  
Wild Type ◽  
Dimeric Form

The nitrate reductase (NADPH) (EC 1.6.6.3) from Aspergillus nidulans is influenced directly by mutations in the structural gene (niaD) for the major subunit of the enzyme and indirectly by mutation in any of several molybdenum cofactor loci (cnx). The cnxE-14 and the cnxH-3 mutants have been noted to contain the enzyme in two distinct forms following induction with nitrate. With the cnxH-3 as a prototype cnxH mutant, 10 other cnxH were found to be devoid of the assembled (dimeric) form of the enzyme. Two monoclonal antibodies specific for the native enzyme of the wild type (biA-1) recognized an epitope on the enzyme from the cnxE-14 and cnxH-3 mutants that was common to both and another that was unique to the cnxH gene specified protomer. Another monoclonal antibody recognized an epitope that occurs only in the assembled dimeric form of the enzyme from the wild type or the cnxE-14 mutant. The experiments further substantiate the cnxH phenotype as one involving unassembled protomers of the nitrate reductase in Aspergillus.

scholarly journals Genetics of nitrate reductase inUstilago maydis

1970 ◽  
Vol 16 (2) ◽  
pp. 151-163 ◽  
Author(s):  
C. M. Lewis ◽  
J. R. S. Fincham
Keyword(s):  
Nitrate Reductase ◽  
Structural Gene ◽  
Nitrate Reduction ◽  
Ustilago Maydis ◽  
Xanthine Dehydrogenase ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Complementation Groups

SUMMARYMutants ofUstilago maydishave been isolated both, deficient and derepressed for nitrate reduction. Those deficient in enzyme fall into six groups, one of which is the structural gene. Enzyme which has proved to be more labile than that of wild-type has been isolated from a temperature-sensitive mutant at this locus. All the mutants in the structural gene have xanthine dehydrogenase activity and the situation closely parallels that ofAspergillus nidulans.The derepressed mutants fall into four complementation groups and all are partially derepressed in that they are further inducible by nitrate. Full derepression can be conferred by induction of a second mutation. In one analysed case the second reinforcing mutation proved to be pheno-typically similar to the first one when separated from it.

Association of the NAD(P)H-bispecific nitrate reductase structural gene with the Nar7 locus in barley

Genome ◽  
1995 ◽  
Vol 38 (4) ◽  
pp. 743-746 ◽  
Author(s):  
R. L. Warner ◽  
D. A. Kudrna ◽  
A. Kleinhofs
Keyword(s):  
Restriction Fragment Length Polymorphism ◽  
Nitrate Reductase ◽  
Structural Gene ◽  
Restriction Fragment ◽  
Length Polymorphism ◽  
Fragment Length ◽  
Fragment Length Polymorphism ◽  
Reductase Activity ◽  
Wild Type ◽  
Restriction Fragment Length

The NADH-specific and NAD(P)H-bispecific nitrate reductase genes from barley have been cloned and sequenced. To determine if the Nar7 locus encodes the NAD(P)H-bispecific nitrate reductase structural gene, a cross was made between a wild-type cultivar, Morex (Nar7 Nar7), and Az70 (nar7w nar7w), a mutant from the cultivar Steptoe that is deficient in NAD(P)H-bispecific nitrate reductase activity. A probe specific to the NAD(P)H-bispecific nitrate reductase structural gene detected restriction fragment length polymorphism between the parents. This probe was used to classify selected F2 progeny for restriction fragment length genotype. All the NAD(P)H nitrate reductase deficient F2 progeny (24/101) possessed the Az70 restriction fragment genotype. The absence of recombination between the NAD(P)H-bispecific nitrate reductase deficient genotype and the NAD(P)H-bispecific nitrate reductase restriction fragment length genotype indicates that the two traits are closely associated in inheritance and that Nar7 is probably the NAD(P)H-bispecific nitrate reductase structural gene.Key words: Hordeum vulgare, nitrate reductase, restriction fragment length polymorphism.

Immunological evidence for transfer of the barley nitrate reductase structural gene to Nicotiana tabacum by protoplast fusion

1986 ◽  
Vol 204 (2) ◽  
pp. 296-301 ◽  
Author(s):  
D. A. Somers ◽  
K. R. Narayanan ◽  
A. Kleinhofs ◽  
S. Cooper-Bland ◽  
E. C. Cocking
Keyword(s):  
Nicotiana Tabacum ◽  
Nitrate Reductase ◽  
Protoplast Fusion ◽  
Structural Gene

scholarly journals A Novel Gene (narM) Required for Expression of Nitrate Reductase Activity in the Cyanobacterium Synechococcus elongatus Strain PCC7942

2004 ◽  
Vol 186 (7) ◽  
pp. 2107-2114 ◽  
Author(s):  
Shin-ichi Maeda ◽  
Tatsuo Omata
Keyword(s):  
Nitrate Reductase ◽  
Structural Gene ◽  
Nitrate Reductase Activity ◽  
Insertional Mutagenesis ◽  
Reductase Activity ◽  
Nitrate Assimilation ◽  
Gene Cassette ◽  
Synechococcus Elongatus ◽  
Prosthetic Group ◽  
Functional Link

ABSTRACT A new class of mutants deficient in nitrate assimilation was obtained from the cyanobacterium Synechococcus elongatus strain PCC7942 by means of random insertional mutagenesis. A 0.5-kb genomic region had been replaced by a kanamycin resistance gene cassette in the mutant, resulting in inactivation of two genes, one of which was homologous to the recently characterized cnaT gene of Anabaena sp. strain PCC7120 (J. E. Frías, A. Herrero, and E. Flores, J. Bacteriol. 185:5037-5044, 2003). While insertional mutation of the cnaT homolog did not affect expression of the nitrate assimilation operon or the activity of the nitrate assimilation enzymes in S. elongatus, inactivation of the other gene, designated narM, resulted in specific loss of the cellular nitrate reductase activity. The deduced NarM protein is a hydrophilic protein consisting of 161 amino acids. narM was expressed constitutively at a low level. The narM gene has its homolog only in the cyanobacterial strains that are capable of nitrate assimilation. In most of the cyanobacterial strains, narM is located downstream of narB, the structural gene of the cyanobacterial nitrate reductase, suggesting the functional link between the two genes. NarM is clearly not the structural component of the cyanobacterial nitrate reductase. The narM insertional mutant normally expressed narB, indicating that narM is not the transcriptional regulator of the structural gene of nitrate reductase. These results suggested that narM is required for either synthesis of the prosthetic group of nitrate reductase or assembly of the prosthetic groups to the NarB polypeptide to form functional nitrate reductase in cyanobacteria.

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