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Query: UNIPROT:P06889 (Mol)
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The nitrate reductase (niaD) gene was isolated from the phytopathogenic loculoascomycete Leptosphaeria maculans by screening a genomic DNA library with the Aspergillus nidulans niaD gene. The L. maculans niaD gene is the first protein-encoding gene characterised from this fungus. It encodes a predicted protein of 893 amino acids and contains four putative introns at positions in the gene equivalent to those of four of the six introns in the A. nidulans niaD gene. Mutants defective in niaD and molybdenum cofactor gene(s) of L. maculans have been isolated. Transformation of a L. maculans niaD mutant with a 3.8 kb SacII fragment containing the L. maculans niaD gene restored wild-type growth on nitrate as a sole nitrogen source. The niaD gene is present as a single copy on a chromosome which ranges in size from 2.6 to 2.8 Mb between the different L. maculans isolates examined.
Mol Gen Genet 1994 Jul 08
PMID:Nitrate reductase of the ascomycetous fungus, Leptosphaeria maculans: gene sequence and chromosomal location. 804 55

The nifQ gene, involved in early stages of iron-molybdenum cofactor (FeMo-co) biosynthesis, was identified downstream of the nifB and nifF genes of Enterobacter agglomerans. This gene was cloned and its nucleotide sequence determined. The amino acid sequence, as deduced from the nucleotide sequence, revealed an accumulation of cysteine amino acid residues at the C-terminal end of the protein. The cysteine cluster showed the following consensus sequence Cys-X4-Cys-X2-Cys-X5-Cys, which is a typical characteristic of metal-binding proteins. Further, the nifQ gene was cloned downstream of strong transcriptional (bacteriophage lambda PLPR) and translational (atpE) signals of the expression vector pCYTEXP1 and expressed as an unfused, soluble protein in Escherichia coli. The molecular mass of 19 kDa, as deduced by SDS-PAGE, is in good agreement with the molecular mass deduced from the nucleotide sequence. The availability of high-level expression clones should facilitate purification of large quantities of the recombinant NifQ protein and elucidation of its properties.
Mol Gen Genet 1993 Jun
PMID:Structure of the nifQ gene from Enterobacter agglomerans 333 and its overexpression in Escherichia coli. 831 14

Tungsten resistant (Wr) mutants of Het+Nif+Nia+, Het+Nif-Nia+ and Het+Nif+Nia- strains of Nostoc muscorum were isolated with severely defective molybdate transport activity. All such mutants showed vanadium (V)-dependent nitrogenase activity and/or nitrate reductase activity and V-dependent growth on N2-nitrogen and/or NO3(-)-nitrogen and V-dependent NO3(-)-repression of heterocyst formation and nitrogenase activity. None of them grew with molybdenum (Mo) under parallel growth condition. Results strongly suggest the ability of V to replace Mo in N2-assimilation or NO3(-)-assimilation under Mo-deficiency.
Biochem Mol Biol Int 1993 Apr
PMID:Mutational replacement of molybdenum by vanadium in assimilation of N2 or NO3- as nitrogen source in the cyanobacterium Nostoc muscorum. 833 16

To identify Rhodobacter capsulatus nif genes necessary for the alternative nitrogenase, strains carrying defined mutations in 32 genes and open reading frames of nif region A, B or C were constructed. The ability of these mutants to grow on nitrogen-free medium with molybdenum (Nif phenotype) or in a nifHDK deletion background on medium without molybdenum (Anf phenotype) was tested. Nine nif genes and nif-associated coding regions are absolutely essential for the alternative nitrogenase. These genes comprise nifV and nifB, the nif-specific ntr system (nifR1, R2, R4) and four open reading frames, which exhibit no homology to known genes. In addition, a significantly reduced activity of both the alternative nitrogenase and the molybdenum-dependent nitrogenase was found for fdxN mutants. By random Tn5 mutagenesis of a nifHDK deletion strain 42 Anf- mutants were isolated. Southern hybridization experiments demonstrated that 17 of these Tn5 mutants were localized in at least 13 different restriction fragments outside of known nif regions. Ten different Anf- Tn5 mutations are clustered on a 6 kb DNA fragment of the chromosome designated anf region A. DNA sequence analysis revealed that this region contained the structural genes of the alternative nitrogenase (anfHDGK). The identification of several Tn5 insertions mapping outside of anf region A indicated that at least 10 genes specific for the alternative nitrogenase are present in R. capsulatus.
Mol Microbiol 1993 May
PMID:Characterization of anf genes specific for the alternative nitrogenase and identification of nif genes required for both nitrogenases in Rhodobacter capsulatus. 833 60

Expression of alternative nitrogenases in Azotobacter vinelandii is repressed by molybdenum. Two strains with Tn5 insertion mutations showed alternative nitrogenase-dependent diazotrophic growth in the presence of Mo. The mutations were in a region which contained four open reading frames (ORFs 1-4). The genetic structure and predicted products of ORFs 2, 3 and 4 are typical of the membrane-associated elements of the ATP-binding cassette (ABC) superfamily of transport systems. The products of ORF3 and ORF4 are homologous with the products of the Escherichia coli genes chlD and the partially sequenced chlJ, respectively, both of which are implicated in molybdenum transport. ORF1, which is in the relative position of bacterial permease genes commonly specifying periplasmic binding proteins, encodes a 29 kDa protein with a novel primary structure. It lacks a potential signal sequence, and its C-terminal half consists of a tandem repeat of a segment which is homologous with the M(r) 7 kDa molybdenum-pterin binding protein Mop from Clostridium pasteurianum. This suggests that a substituted pterin may be involved in the initial capture or early metabolism of molybdenum.
Mol Microbiol 1993 Feb
PMID:Characterization of genes involved in molybdenum transport in Azotobacter vinelandii. 838 83

Nitrate reductase of Neurospora crassa is a dimeric protein composed of two identical subunits, each possessing three separate domains, with flavin, heme, and molybdenum-containing cofactors. A number of mutants of nit-3, the structural gene that encodes Neurospora nitrate reductase, have been characterized at the molecular level. Amber nonsense mutants of nit-3 were found to possess a truncated protein detected by a specific antibody, whereas Ssu-1-suppressed nonsense mutants showed restoration of the wild-type, full-length nitrate reductase monomer. The mutants show constitutive expression of the truncated nitrate reductase protein; however normal control, which requires nitrate induction, was restored in the suppressed mutant strains. Three conventional nit-3 mutants were isolated by the polymerase chain reaction and sequenced; two of these mutants were due to the deletion of a single base in the coding region for the flavin domain, the third mutant was a nonsense mutation within the amino-terminal molybdenum-containing domain. Homologous recombination was shown to occur when a deleted nit-3 gene was introduced by transformation into a host strain with a single point mutation in the resident nit-3 gene. New, severely damaged, null nit-3 mutants were created by repeat-induced point mutation and demonstrated to be useful as host strains for transformation experiments.
Mol Gen Genet 1993 Apr
PMID:Molecular characterization of conventional and new repeat-induced mutants of nit-3, the structural gene that encodes nitrate reductase in Neurospora crassa. 847 43

DNA sequence analysis of a 3494-bp HindIII-BclI fragment of the Rhodobacter capsulatus nif region A revealed genes that are homologous to ORF6, nifU, nifS, nifV and nifW from Azotobacter vinelandii and Klebsiella pneumoniae. R. capsulatus nifU, which is present in two copies, encodes a novel type of NifU protein. The deduced amino acid sequences of NifUI and NifUII share homology only with the C-terminal domain of NifU from A. vinelandii and K. pneumoniae. In contrast to nifA and nifB, which are almost perfectly duplicated, the predicted amino acid sequences of the two NifU proteins showed only 39% sequence identity. Expression of the ORF6-nifUISVW operon, which is preceded by a putative sigma 54-dependent promoter, required the function of NifA and the nif-specific rpoN gene product encoded by nifR4. Analysis of defined insertion and deletion mutants demonstrated that only nifS was absolutely essential for nitrogen fixation in R. capsulatus. Strains carrying mutations in nifV were capable of very slow diazotrophic growth, whereas ORF6, nifUI and nifW mutants as well as a nifUI/nifUII double mutant exhibited a Nif+ phenotype. Interestingly, R. capsulatus nifV mutants were able to reduce acetylene not only to ethylene but also to ethane under conditions preventing the expression of the alternative nitrogenase system. Homocitrate added to the growth medium repressed ethane formation and cured the NifV phenotype in R. capsulatus. Higher concentrations of homocitrate were necessary to complement the NifV phenotype of a polar nifV mutant (NifV-NifW-), indicating a possible role of NifW either in homocitrate transport or in the incorporation of this compound into the iron-molybdenum cofactor of nitrogenase.
Mol Gen Genet 1993 Apr
PMID:Nucleotide sequence and genetic analysis of the Rhodobacter capsulatus ORF6-nifUI SVW gene region: possible role of NifW in homocitrate processing. 849 5

Mutant plants defective in the assimilation of nitrate can be selected by their resistance to the herbicide chlorate. In Arabidopsis thaliana, mutations at any one of nine distinct loci confer chlorate resistance. Only one of the CHL genes, CHL3, has been shown genetically to be a nitrate reductase (NR) structural gene (NIA2) even though two NR genes (NIA1 and NIA2) have been cloned from the Arabidopsis genome. Plants in which the NIA2 gene has been deleted retain only 10% of the wild-type shoot NR activity and grow normally with nitrate as the sole nitrogen source. Using mutagenized seeds from the NIA2 deletion mutant and a modified chlorate selection protocol, we have identified the first mutation in the NIA1 NR structural gene. nia1, nia2 double mutants have only 0.5% of wild-type shoot NR activity and display very poor growth on media with nitrate as the only form of nitrogen. The nia1-1 mutation is a single nucleotide substitution that converts an alanine to a threonine in a highly conserved region of the molybdenum cofactor-binding domain of the NR protein. These results show that the NIA1 gene encodes a functional NR protein that contributes to the assimilation of nitrate in Arabidopsis.
Mol Gen Genet 1993 May
PMID:Identification and characterization of a chlorate-resistant mutant of Arabidopsis thaliana with mutations in both nitrate reductase structural genes NIA1 and NIA2. 851 Jun 58

Upon incubation in rabbit reticulocyte lysate, the unactivated progesterone receptor (PR) associates with the heat shock proteins hsp90 and hsp70, the immunophilins FKBP52, FKBP54, and CyP-40, and another protein p23. We have previously described a protein complex between p23, hsp90, and the immunophilins that forms in rabbit reticulocyte lysate in the absence of the PR. Immunodepletion of p23 from lysate prevented the binding of hsp90 and CyP-40 to the PR, suggesting that hsp90, CyP-40, and p23 bind the receptor as a complex. We have further examined the properties of this p23 complex to determine how it is involved in receptor assembly in vitro. Use was made of three chemical probes, sodium molybdate, the nonhydrolyzable ATP analog, 5'-adenylylimidodiphosphate, and the hsp90-binding agent geldanamycin. Molybdate has previously been shown to stabilize the heat-induced dissociation of hsp90 and p23 from the PR. This stabilization is not mediated through the PR, as molybdate stabilizes the heat-induced dissociation of hsp90 from p23 even in the absence of the PR. Molybdate also stabilizes both p23 and PR complexes under conditions of low ATP and magnesium concentration. The ATP analog, 5'-adenylylimidodiphosphate, which does not support the assembly of PR complexes, promotes both the assembly and stabilization of p23 complexes. Geldanamycin disrupts p23 complexes, and when PR complexes are treated with this agent, p23, CyP-40, and some hsp90 are lost from the receptor. Thus, all three of these chemical agents appear to target the p23 complex, which is thought to enter at the last step in the assembly of the PR complex. A model is presented to relate these findings to previous models and another complex between hsp90, hsp70, and p60 that appears to be an intermediate in PR assembly.
Mol Endocrinol 1995 Jun
PMID:Binding of p23 and hsp90 during assembly with the progesterone receptor. 859 13

Two different fdxH genes (fdxH1, fdxH2) have been isolated from the nitrogen-fixing, heterocyst-forming cyanobacterium Anabaena variabilis ATCC 29413. They are part of two different nif gene clusters, nif1 and nif2. fdxH1 encodes the [2Fe-2S] ferredoxin that is known as the direct electron donor to nitrogenase in heterocysts, and is very similar to FdxH from Anabaena sp. PCC 7120. FdxH2 has more residues in common and shares its oxygen sensitivity with the single FdxH from the non-heterocystous, filamentous cyanobacterium Plectonema boryanum PCC 73110. The latter expresses nitrogenase early (< or = 3-4h) after nitrogen depletion in vegetative cells and exclusively under anaerobic conditions. fdxH2 and the nif2 genes of Anabaena 29413 are also transcribed < or = 4 h after onset of nitrogen-stepdown, exclusively under anaerobic growth conditions and long before functional heterocysts appear. At this time, no fdxH1 and nif1 gene transcription was observed. It occurred later and was associated with nitrogen fixation under aerobic conditions, i.e. within heterocysts. fdxH2 and nifHDK2 were not transcribed during aerobic, nitrogen-fixing growth. In addition, neither was an fdxH2-type gene found nor an anaerobically and early inducible Nif2 system detectable in Anabaena 7120. These data reveal that in filamentous cyanobacteria two different Nif systems have evolved based on molybdenum nitrogenases. It is concluded that a Nif2-type system operates in vegetative cells of non-heterocystous and some, but not all, heterocyst-forming filamentous cyanobacteria. It is environmentally regulated by the levels of both oxygen and combined nitrogen in the habitat. To simultaneously allow for oxygen-evolving photosynthesis and oxygen-sensitive nitrogen fixation, the Nif1-type system probably branched from an ancestral Nif2-type system and has evolved for an exclusive operation within heterocysts. Accordingly, its expression has become an obligate late event in the developmental programme of heterocyst differentiation, irrespective of aerobic or anaerobic growth conditions.
Mol Microbiol 1995 Oct
PMID:Distinct and differently regulated Mo-dependent nitrogen-fixing systems evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC 29413: characterization of the fdxH1/2 gene regions as part of the nif1/2 gene clusters. 870 54


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