Dataset Information

Dopaminium nitrate.

ABSTRACT: THE ASYMMETRIC UNIT OF THE TITLE SALT [SYSTEMATIC NAME: 2-(3,4-di-hydroxy-phen-yl)ethanaminium nitrate], C8H12NO2 (+)·NO3 (-), contains two independent cations and two independent nitrate anions. The crystal structure consists of discrete nitrate ions stacked in layers parallel to (010). These layers are linked via the dopaminium cations by O-H?O, N-H?O and weak C-H?O hydrogen bonds, forming a three-dimensional supra-molecular network.

SUBMITTER: Gatfaoui S

PROVIDER: S-EPMC4011303 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Dopaminium nitrate.

Gatfaoui Sofian S Marouani Houda H Roisnel Thierry T Dhaouadi Hassouna H

Acta crystallographica. Section E, Structure reports online 20140418 Pt 5

THE ASYMMETRIC UNIT OF THE TITLE SALT [SYSTEMATIC NAME: 2-(3,4-di-hydroxy-phen-yl)ethanaminium nitrate], C8H12NO2 (+)·NO3 (-), contains two independent cations and two independent nitrate anions. The crystal structure consists of discrete nitrate ions stacked in layers parallel to (010). These layers are linked via the dopaminium cations by O-H⋯O, N-H⋯O and weak C-H⋯O hydrogen bonds, forming a three-dimensional supra-molecular network. ...[more]

PMID: 24860376

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Project description:In fungi, transcriptional activation of genes involved in NO3(-) assimilation requires the presence of an inducer (nitrate or nitrite) and low intracellular concentrations of the pathway products ammonium or glutamine. In Aspergillus nidulans, the two transcription factors NirA and AreA act synergistically to mediate nitrate/nitrite induction and nitrogen metabolite derepression, respectively. In all studied fungi and in plants, mutants lacking nitrate reductase (NR) activity express nitrate-metabolizing enzymes constitutively without the addition of inducer molecules. Based on their work in A. nidulans, Cove and Pateman proposed an "autoregulation control" model for the synthesis of nitrate metabolizing enzymes in which the functional nitrate reductase molecule would act as co-repressor in the absence and as co-inducer in the presence of nitrate. However, NR mutants could simply show "pseudo-constitutivity" due to induction by nitrate which accumulates over time in NR-deficient strains. Here we examined this possibility using strains which lack flavohemoglobins (fhbs), and are thus unable to generate nitrate internally, in combination with nitrate transporter mutations (nrtA, nrtB) and a GFP-labeled NirA protein. Using different combinations of genotypes we demonstrate that nitrate transporters are functional also in NR null mutants and show that the constitutive phenotype of NR mutants is not due to nitrate accumulation from intracellular sources but depends on the activity of nitrate transporters. However, these transporters are not required for nitrate signaling because addition of external nitrate (10 mM) leads to standard induction of nitrate assimilatory genes in the nitrate transporter double mutants. We finally show that NR does not regulate NirA localization and activity, and thus the autoregulation model, in which NR would act as a co-repressor of NirA in the absence of nitrate, is unlikely to be correct. Results from this study instead suggest that transporter-mediated NO?? accumulation in NR deficient mutants, originating from traces of nitrate in the media, is responsible for the constitutive expression of NirA-regulated genes, and the associated phenotype is thus termed "pseudo-constitutive".

Dataset Information

Dopaminium nitrate.

Publications

Dopaminium nitrate.

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