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Pesquisa : D08.811.682.655.750.500 [Categoria DeCS]
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  1 / 24 MEDLINE  
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[PMID]:27838765
[Au] Autor:Liu X; Chen CR; Hughes JM; Wang WJ; Lewis T
[Ad] Endereço:College of Forestry, Fujian Agriculture and Forestry University, Fuzhou, 350002, China. xianliu@fafu.edu.cn.
[Ti] Título:Temporal Changes Rather than Long-Term Repeated Burning Predominately Control the Shift in the Abundance of Soil Denitrifying Community in an Australian Sclerophyll Forest.
[So] Source:Microb Ecol;73(1):177-187, 2017 Jan.
[Is] ISSN:1432-184X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To understand the temporal dynamics of soil bacterial denitrifying community in response to long-term prescribed burning and its resilience and recovery following a fire, a wet sclerophyll forest study site under two treatments (2 yearly burning (2YB) and no burning (NB)) and with 40-year-old burning history was used. Similar temporal patterns in the abundance of total (16S rRNA) and denitrifying (narG, nirK, nirS, nosZ) bacteria between two burning treatments revealed strong temporal influences. The magnitude of burning impacts on the abundance of 16S rRNA and denitrification genes was smaller compared with the impact of sampling time, but significant burning and temporal impacts were recorded for all (P < 0.001)-except for the nirS gene. Impacts of prescribed fire on the abundance of soil denitrifying community could be observed immediately after fire, and this impact diminished over a 24-month period prior to the next prescribed burning event. In conclusion, temporal changes govern the fluctuations of the abundance of soil denitrifying genes over the sampling period and the denitrifying community can recover after fire, suggesting that this community is resilient to the effects of prescribed burning. A combination of biotic and abiotic factors may account for the different temporal dynamics of denitrification gene abundance.
[Mh] Termos MeSH primário: Bactérias/classificação
Bactérias/metabolismo
Microbiologia do Solo
Solo/química
Árvores/microbiologia
[Mh] Termos MeSH secundário: Austrália
Bactérias/genética
Desnitrificação
Fogo
Florestas
Nitrito Redutase (NAD(P)H)/genética
Oxirredutases/genética
RNA Ribossômico 16S/genética
Chuvas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 16S); 0 (Soil); EC 1.- (Oxidoreductases); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); EC 1.7.2.4 (nitrous oxide reductase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161114
[St] Status:MEDLINE
[do] DOI:10.1007/s00248-016-0894-6


  2 / 24 MEDLINE  
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[PMID]:24005668
[Au] Autor:Luque-Almagro VM; Lyall VJ; Ferguson SJ; Roldán MD; Richardson DJ; Gates AJ
[Ad] Endereço:From the Centre for Molecular and Structural Biochemistry and.
[Ti] Título:Nitrogen oxyanion-dependent dissociation of a two-component complex that regulates bacterial nitrate assimilation.
[So] Source:J Biol Chem;288(41):29692-702, 2013 Oct 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitrogen is an essential nutrient for growth and is readily available to microbes in many environments in the form of ammonium and nitrate. Both ions are of environmental significance due to sustained use of inorganic fertilizers on agricultural soils. Diverse species of bacteria that have an assimilatory nitrate/nitrite reductase system (NAS) can use nitrate or nitrite as the sole nitrogen source for growth when ammonium is limited. In Paracoccus denitrificans, the pathway-specific two-component regulator for NAS expression is encoded by the nasT and nasS genes. Here, we show that the putative RNA-binding protein NasT is a positive regulator essential for expression of the nas gene cluster (i.e. nasABGHC). By contrast, a nitrogen oxyanion-binding sensor (NasS) is required for nitrate/nitrite-responsive control of nas gene expression. The NasS and NasT proteins co-purify as a stable heterotetrameric regulatory complex, NasS-NasT. This protein-protein interaction is sensitive to nitrate and nitrite, which cause dissociation of the NasS-NasT complex into monomeric NasS and an oligomeric form of NasT. NasT has been shown to bind the leader RNA for nasA. Thus, upon liberation from the complex, the positive regulator NasT is free to up-regulate nas gene expression.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Proteínas de Bactérias/metabolismo
Nitratos/metabolismo
Nitrogênio/metabolismo
[Mh] Termos MeSH secundário: Ânions/química
Bactérias/genética
Bactérias/crescimento & desenvolvimento
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Eletroforese em Gel de Poliacrilamida
Regulação Bacteriana da Expressão Gênica
Cinética
Família Multigênica
Mutação
Nitrito Redutase (NAD(P)H)/química
Nitrito Redutase (NAD(P)H)/genética
Nitrito Redutase (NAD(P)H)/metabolismo
Nitritos/metabolismo
Nitrogênio/química
Oxigênio/química
Paracoccus denitrificans/genética
Paracoccus denitrificans/metabolismo
Ligação Proteica
Multimerização Proteica
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
Transdução de Sinais/genética
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anions); 0 (Bacterial Proteins); 0 (Nitrates); 0 (Nitrites); 0 (RNA, Bacterial); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); N762921K75 (Nitrogen); S88TT14065 (Oxygen)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130906
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M113.459032


  3 / 24 MEDLINE  
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[PMID]:22976986
[Au] Autor:Nakano S; Takahashi M; Sakamoto A; Morikawa H; Katayanagi K
[Ad] Endereço:Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1, Kagamiyama, Higashi-Hiroshima 739-8526, Japan.
[Ti] Título:X-ray crystal structure of a mutant assimilatory nitrite reductase that shows sulfite reductase-like activity.
[So] Source:Chem Biodivers;9(9):1989-99, 2012 Sep.
[Is] ISSN:1612-1880
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Assimilatory nitrite reductase (aNiR) reduces nitrite ions (NO(2)(-)) to ammonium ions (NH(4)(+)), whereas assimilatory sulfite reductase reduces sulfite (SO(3)(2-)) to hydrogen sulfide (HS(-)). Although aNiR can also reduce SO(3)(2-), its activity is much lower than when NO(2)(-) is reduced as the substrate. To increase the SO(3)(2-)-reduction activity of aNiR, we performed a N226K mutation of Nii3, a representative aNiR. The resulting Nii3-N226K variant could bind non-native targets, SO(3)(2-), and HCO(3)(-), in addition to its native target, i.e., NO(2)(-). We have determined the high-resolution structure of Nii3-N226K in its apo-state and in complex with SO(3)(2-), NO(2)(-), and HCO(3)(-). This analysis revealed conformational changes of Lys226 and the adjacent Lys224 upon binding of SO(3)(2-), but not NO(2)(-)In contrast, HCO(3)(-) binding induced a conformational change at Arg179. After replacing Asn226 with a positively charged Lys, aNiR showed affinity for several anions. A comparison of all ligand-bound structures for Nii3-N226K revealed that structural changes in the active site depend on the size of the substrate.
[Mh] Termos MeSH primário: Modelos Moleculares
Mutação
Nitrito Redutase (NAD(P)H)/química
Nitrito Redutase (NAD(P)H)/genética
Sulfitos/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Nitrito Redutase (NAD(P)H)/metabolismo
Oxirredutases/química
Oxirredutases/metabolismo
Sulfitos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Sulfites); EC 1.- (Oxidoreductases); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H))
[Em] Mês de entrada:1301
[Cu] Atualização por classe:120914
[Lr] Data última revisão:
120914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120915
[St] Status:MEDLINE
[do] DOI:10.1002/cbdv.201100442


  4 / 24 MEDLINE  
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[PMID]:22534036
[Au] Autor:Karsh KL; Granger J; Kritee K; Sigman DM
[Ad] Endereço:Department of Geosciences, Princeton University, Guyot Hall, Princeton, New Jersey 08544, United States. Kristen.Karsh@csiro.au
[Ti] Título:Eukaryotic assimilatory nitrate reductase fractionates N and O isotopes with a ratio near unity.
[So] Source:Environ Sci Technol;46(11):5727-35, 2012 Jun 05.
[Is] ISSN:1520-5851
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In order to (i) establish the biological systematics necessary to interpret nitrogen (N) and oxygen (O) isotope ratios of nitrate ((15)N/(14)N and (18)O/(16)O) in the environment and (ii) investigate the potential for isotopes to elucidate the mechanism of a key N cycle enzyme, we measured the nitrate N and O isotope effects ((15)ε and (18)ε) for nitrate reduction by two assimilatory eukaryotic nitrate reductase (eukNR) enzymes. The (15)ε for purified extracts of NADPH eukNR from the fungus Aspergillus niger and the (15)ε for NADH eukNR from cell homogenates of the marine diatom Thalassiosira weissflogii were indistinguishable, yielding a mean (15)ε for the enzyme of 26.6 ± 0.2‰. Both forms of eukNR imparted near equivalent fractionation on N and O isotopes. The increase in (18)O/(16)O versus the increase in (15)N/(14)N (relative to their natural abundances) was 0.96 ± 0.01 for NADPH eukNR and 1.09 ± 0.03 for NADH eukNR. These results are the first reliable measurements of the coupled N and O isotope effects for any form of eukNR. They support the prevailing view that intracellular reduction by eukNR is the dominant step in isotope fractionation during nitrate assimilation and that it drives the (18)ε:(15)ε ≈ 1 observed in phytoplankton cultures, suggesting that this O-to-N isotope signature will apply broadly in the environment. Our measured (15)ε and (18)ε may represent the intrinsic isotope effects for eukNR-mediated N-O bond rupture, a potential constraint on the nature of the enzyme's transition state.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Diatomáceas/enzimologia
Células Eucarióticas/enzimologia
Nitrito Redutase (NAD(P)H)/metabolismo
Nitrogênio/metabolismo
Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Fracionamento Químico
Elétrons
Ensaios Enzimáticos
NAD/metabolismo
NADP/metabolismo
Nitratos/análise
Isótopos de Nitrogênio
Isótopos de Oxigênio
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Nitrates); 0 (Nitrogen Isotopes); 0 (Oxygen Isotopes); 0U46U6E8UK (NAD); 53-59-8 (NADP); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); N762921K75 (Nitrogen); S88TT14065 (Oxygen)
[Em] Mês de entrada:1209
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120427
[St] Status:MEDLINE
[do] DOI:10.1021/es204593q


  5 / 24 MEDLINE  
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[PMID]:22238192
[Au] Autor:Nakano S; Takahashi M; Sakamoto A; Morikawa H; Katayanagi K
[Ad] Endereço:Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
[Ti] Título:Structure-function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high-resolution structures.
[So] Source:Protein Sci;21(3):383-95, 2012 Mar.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tobacco expresses four isomers of assimilatory nitrite reductase (aNiR), leaf-type (Nii1 and Nii3), and root-type (Nii2 and Nii4). The high-resolution crystal structures of Nii3 and Nii4, determined at 1.25 and 2.3 Å resolutions, respectively, revealed that both proteins had very similar structures. The Nii3 structure provided detailed geometries for the [4Fe-4S] cluster and the siroheme prosthetic groups. We have generated two types of Nii3 variants: one set focuses on residue Met175 (Nii3-M175G, Nii3-M175E, and Nii3-M175K), a residue that is located on the substrate entrance pathway; the second set targets residue Gln448 (Nii3-Q448K), a residue near the prosthetic groups. Comparison of the structures and kinetics of the Nii3 wild-type (Nii3-WT) and the Met175 variants showed that the hydrophobic side-chain of Met175 facilitated enzyme efficiency (k(cat) /K(m) ). The Nii4-WT has Lys449 at the equivalent position of Gln448 in Nii3-WT. The enzyme activity assay revealed that the turnover number (k(cat) ) and Michaelis constant (K(m) ) of Nii4-WT were lower than those of Nii3-WT. However, the k(cat) /K(m) of Nii4-WT was about 1.4 times higher than that of Nii3-WT. A comparison of the kinetics of the Nii3-Q448K and Nii4-K449Q variants revealed that the change in k(cat) /K(m) was brought about by the difference in Residue 448 (defined as Gln448 in Nii3 and Lys449 in Nii4). By combining detailed crystal structures with enzyme kinetics, we have proposed that Nii3 is the low-affinity and Nii4 is the high-affinity aNiR.
[Mh] Termos MeSH primário: Nitrito Redutase (NAD(P)H)/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Cinética
Modelos Moleculares
Dados de Sequência Molecular
Nitrito Redutase (NAD(P)H)/química
Nitrito Redutase (NAD(P)H)/genética
Folhas de Planta/enzimologia
Raízes de Plantas/enzimologia
Alinhamento de Sequência
Relação Estrutura-Atividade
Tabaco
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.7.1.4 (Nitrite Reductase (NAD(P)H))
[Em] Mês de entrada:1206
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120113
[St] Status:MEDLINE
[do] DOI:10.1002/pro.2025


  6 / 24 MEDLINE  
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[PMID]:21424691
[Au] Autor:Shao Z; Gao J; Ding X; Wang J; Chiao J; Zhao G
[Ad] Endereço:Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:Identification and functional analysis of a nitrate assimilation operon nasACKBDEF from Amycolatopsis mediterranei U32.
[So] Source:Arch Microbiol;193(7):463-77, 2011 Jul.
[Is] ISSN:1432-072X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Nitrate assimilation has been well studied for Gram-negative bacteria but not so much in the Gram-positive actinomycetes up to date. In a rifamycin SV-producing actinomycete, Amycolatopsis mediterranei strain U32, nitrate not only can be used as a sole nitrogen source but also remarkably stimulates the antibiotic production along with regulating the related metabolic enzymes. A gene cluster of nasACKBDEF was cloned from a U32 genomic library by in situ hybridization screening with a heterogeneous nasB probe and confirmed later by whole genome sequence, corresponding to the protein coding genes of AMED_1121 to AMED_1127. These genes were co-transcribed as an operon, concomitantly repressed by ammonium while activated with supplement of either nitrate or nitrite. Genetic and biochemical analyses identified the essential nitrate/nitrite assimilation functions of the encoded proteins, orderly, the assimilatory nitrate reductase catalytic subunit (NasA), nitrate reductase electron transfer subunit (NasC), nitrate/nitrite transporter (NasK), assimilatory nitrite reductase large subunit (NasB) and small subunit (NasD), bifunctional uroporphyrinogen-III synthase (NasE), and an unknown function protein (NasF). Comparing rifamycin SV production and the level of transcription of nasB and rifE from U32 and its individual nas mutants in Bennet medium with or without nitrate indicated that nitrate assimilation function encoded by the nas operon played an essential role in the "nitrate stimulated" rifamycin production but had no effect upon the transcription regulation of the primary and secondary metabolic genes related to rifamycin biosynthesis.
[Mh] Termos MeSH primário: Actinomycetales/genética
Família Multigênica
Nitratos/metabolismo
Nitrito Redutase (NAD(P)H)/genética
Óperon
[Mh] Termos MeSH secundário: Actinomycetales/enzimologia
Actinomycetales/crescimento & desenvolvimento
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clonagem Molecular
DNA Bacteriano/genética
Regulação Bacteriana da Expressão Gênica
Teste de Complementação Genética
Mutação
Nitrito Redutase (NAD(P)H)/metabolismo
Nitritos/metabolismo
Nitrogênio/metabolismo
Rifamicinas/biossíntese
Análise de Sequência de DNA
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Nitrates); 0 (Nitrites); 0 (Rifamycins); DU69T8ZZPA (rifamycin SV); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); N762921K75 (Nitrogen)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110323
[St] Status:MEDLINE
[do] DOI:10.1007/s00203-011-0690-0


  7 / 24 MEDLINE  
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[PMID]:17572840
[Au] Autor:Martínez-Espinosa RM; Lledó B; Marhuenda-Egea FC; Bonete MJ
[Ad] Endereço:División de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Alicante, Ap. 99, 03080, Alicante, Spain. rosa.martinez@ua.es
[Ti] Título:The effect of ammonium on assimilatory nitrate reduction in the haloarchaeon Haloferax mediterranei.
[So] Source:Extremophiles;11(6):759-67, 2007 Nov.
[Is] ISSN:1431-0651
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Physiology, regulation and biochemical aspects of the nitrogen assimilation are well known in Prokarya or Eukarya but they are poorly described in Archaea domain. The haloarchaeon Haloferax mediterranei can use different nitrogen inorganic sources (NO (3) (-) , NO (2) (-) or NH (4) (+) ) for growth. Different approaches were considered to study the effect of NH (4) (+) on nitrogen assimilation in Hfx. mediterranei cells grown in KNO(3) medium. The NH (4) (+) addition to KNO(3) medium caused a decrease of assimilatory nitrate (Nas) and nitrite reductases (NiR) activities. Similar effects were observed when nitrate-growing cells were transferred to NH (4) (+) media. Both activities increased when NH (4) (+) was removed from culture, showing that the negative effect of NH (4) (+) on this pathway is reversible. These results suggest that ammonium causes the inhibition of the assimilatory nitrate pathway, while nitrate exerts a positive effect. This pattern has been confirmed by RT-PCR. In the presence of both NO (3) (-) and NH (4) (+) , NH (4) (+) was preferentially consumed, but NO (3) (-) uptake was not completely inhibited by NH (4) (+) at prolonged time scale. The addition of MSX to NH (4) (+) or NO (3) (-) cultures results in an increase of Nas and NiR activities, suggesting that NH (4) (+) assimilation, rather than NH (4) (+ ) per se, has a negative effect on assimilatory nitrate reduction in Hfx. mediterranei.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Haloferax mediterranei/metabolismo
Nitrato Redutase (NADPH)/metabolismo
Nitratos/metabolismo
Nitrito Redutase (NAD(P)H)/metabolismo
Fixação de Nitrogênio
Compostos de Amônio Quaternário/metabolismo
[Mh] Termos MeSH secundário: Meios de Cultura Livres de Soro/metabolismo
Indução Enzimática
Regulação da Expressão Gênica em Archaea
Haloferax mediterranei/enzimologia
Haloferax mediterranei/crescimento & desenvolvimento
Metionina Sulfoximina/metabolismo
Nitrato Redutase (NADPH)/biossíntese
Nitrato Redutase (NADPH)/genética
Nitrito Redutase (NAD(P)H)/biossíntese
Nitrito Redutase (NAD(P)H)/genética
Nitritos/metabolismo
Oxirredução
Compostos de Potássio/metabolismo
RNA Mensageiro/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Culture Media, Serum-Free); 0 (Nitrates); 0 (Nitrites); 0 (Potassium Compounds); 0 (Quaternary Ammonium Compounds); 0 (RNA, Messenger); 1982-67-8 (Methionine Sulfoximine); EC 1.7.1.3 (Nitrate Reductase (NADPH)); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); RU45X2JN0Z (potassium nitrate); T8YA51M7Y6 (ammonium nitrate)
[Em] Mês de entrada:0803
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:070619
[St] Status:MEDLINE


  8 / 24 MEDLINE  
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[PMID]:9765565
[Au] Autor:Nakano MM; Hoffmann T; Zhu Y; Jahn D
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, Shreveport, Louisiana 71130-3932, USA mnakano @bmb.ogi.edu
[Ti] Título:Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE.
[So] Source:J Bacteriol;180(20):5344-50, 1998 Oct.
[Is] ISSN:0021-9193
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nitrate and nitrite reductases of Bacillus subtilis have two different physiological functions. Under conditions of nitrogen limitation, these enzymes catalyze the reduction of nitrate via nitrite to ammonia for the anabolic incorporation of nitrogen into biomolecules. They also function catabolically in anaerobic respiration, which involves the use of nitrate and nitrite as terminal electron acceptors. Two distinct nitrate reductases, encoded by narGHI and nasBC, function in anabolic and catabolic nitrogen metabolism, respectively. However, as reported herein, a single NADH-dependent, soluble nitrite reductase encoded by the nasDE genes is required for both catabolic and anabolic processes. The nasDE genes, together with nasBC (encoding assimilatory nitrate reductase) and nasF (required for nitrite reductase siroheme cofactor formation), constitute the nas operon. Data presented show that transcription of nasDEF is driven not only by the previously characterized nas operon promoter but also from an internal promoter residing between the nasC and nasD genes. Transcription from both promoters is activated by nitrogen limitation during aerobic growth by the nitrogen regulator, TnrA. However, under conditions of oxygen limitation, nasDEF expression and nitrite reductase activity were significantly induced. Anaerobic induction of nasDEF required the ResDE two-component regulatory system and the presence of nitrite, indicating partial coregulation of NasDEF with the respiratory nitrate reductase NarGHI during nitrate respiration.
[Mh] Termos MeSH primário: Bacillus subtilis/genética
Proteínas de Ligação a DNA
Nitrito Redutases/biossíntese
Nitrogênio/farmacologia
Oxigênio/farmacologia
Proteínas Repressoras
[Mh] Termos MeSH secundário: Aerobiose
Anaerobiose
Bacillus subtilis/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sequência de Bases
Indução Enzimática
Repressão Enzimática
Regulação Bacteriana da Expressão Gênica
Genes Bacterianos
Genes Reporter
Histidina Quinase
Dados de Sequência Molecular
Nitrato Redutase
Nitrato Redutases/genética
Nitrito Redutase (NAD(P)H)
Consumo de Oxigênio
Regiões Promotoras Genéticas
Proteínas Quinases/genética
Proteínas Quinases/metabolismo
Transdução de Sinais
Fatores de Transcrição/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA-Binding Proteins); 0 (Repressor Proteins); 0 (ResD protein, Bacillus subtilis); 0 (ScgR protein, Bacillus subtilis); 0 (Transcription Factors); EC 1.7.- (Nitrate Reductases); EC 1.7.- (Nitrite Reductases); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); EC 1.7.99.4 (Nitrate Reductase); EC 2.7.- (Protein Kinases); EC 2.7.13.1 (Histidine Kinase); N762921K75 (Nitrogen); S88TT14065 (Oxygen)
[Em] Mês de entrada:9810
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:981010
[St] Status:MEDLINE


  9 / 24 MEDLINE  
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[PMID]:9547218
[Au] Autor:Sengupta S; Subbarap Shaila M; Rao GR
[Ad] Endereço:Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
[Ti] Título:In vitro and in vivo regulation of assimilatory nitrite reductase from Candida utilis.
[So] Source:Arch Microbiol;168(3):215-24, 1997 Sep.
[Is] ISSN:0302-8933
[Cp] País de publicação:Germany
[La] Idioma:eng
[Mh] Termos MeSH primário: Candida/enzimologia
Nitrito Redutases/metabolismo
[Mh] Termos MeSH secundário: Cloreto de Amônio/farmacologia
Candida/crescimento & desenvolvimento
Cloromercurobenzoatos/farmacologia
Cisteína/antagonistas & inibidores
Indução Enzimática
Repressão Enzimática
Flavina-Adenina Dinucleotídeo/farmacologia
Regulação Enzimológica da Expressão Gênica
Cinética
NAD/metabolismo
NADP/metabolismo
Nitrito Redutase (NAD(P)H)
Nitrito Redutases/biossíntese
Ácido p-Cloromercurobenzoico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chloromercuribenzoates); 01Q9PC255D (Ammonium Chloride); 0U46U6E8UK (NAD); 146-14-5 (Flavin-Adenine Dinucleotide); 53-59-8 (NADP); 59-85-8 (p-Chloromercuribenzoic Acid); EC 1.7.- (Nitrite Reductases); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H)); K848JZ4886 (Cysteine)
[Em] Mês de entrada:9804
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:980418
[St] Status:MEDLINE


  10 / 24 MEDLINE  
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[PMID]:9382703
[Au] Autor:Tyson K; Busby S; Cole J
[Ad] Endereço:School of Biochemistry, University of Birmingham, Birmingham B15 2TT, UK.
[Ti] Título:Catabolite regulation of two Escherichia coli operons encoding nitrite reductases: role of the Cra protein.
[So] Source:Arch Microbiol;168(3):240-4, 1997 Sep.
[Is] ISSN:0302-8933
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The Escherichia coli nir and nrf operons, which encode alternative nitrite reductases expressed during anaerobic growth, are subject to catabolite regulation. Transcription from the nir promoter is maximal when bacteria are grown in rich media such as Lennox broth supplemented with glucose. Conversely, expression of the nrf operon is suppressed by rich media, but stimulated during growth in minimal medium with glycerol and fumarate. The role of the catabolite repressor-activator (Cra) protein in catabolite regulation of the nir and nrf promoters was investigated. Transcription from the nir promoter was repressed by Cra when cells were grown in minimal medium with glycerol and fumarate. Crude protein extracts from a strain overproducing Cra encoded on a multicopy plasmid retarded a nir promoter fragment in a mobility shift assay, confirming that the observed Cra-dependent repression was due to the direct interaction of Cra with the regulatory region of the nir operon. Furthermore, the inclusion of fructose 1-phosphate, an effector of Cra DNA-binding activity, in the assay decreased the ability of Cra to retard the nir promoter fragment. In contrast, transcription from the nrf promoter was not regulated by Cra under any of the growth conditions tested.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Proteínas de Escherichia coli
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Nitrito Redutases/genética
Óperon
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ligação a DNA/metabolismo
Repressão Enzimática
Escherichia coli/enzimologia
Frutosefosfatos/farmacologia
Nitrito Redutase (NAD(P)H)
Nitrito Redutases/biossíntese
Regiões Promotoras Genéticas
Ligação Proteica/efeitos dos fármacos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA-Binding Proteins); 0 (Escherichia coli Proteins); 0 (FruR protein, E coli); 0 (Fructosephosphates); 0 (Repressor Proteins); 138186-82-0 (FruR protein, Bacteria); 15978-08-2 (fructose-1-phosphate); EC 1.7.- (Nitrite Reductases); EC 1.7.1.4 (Nitrite Reductase (NAD(P)H))
[Em] Mês de entrada:9711
[Cu] Atualização por classe:081121
[Lr] Data última revisão:
081121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:970908
[St] Status:MEDLINE



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