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UniProt Q9K4V0 corresponds to NorR1, a nitric-oxide (NO) responsive transcriptional activator in Cupriavidus necator (syn. Ralstonia eutropha) strain H16. Primary literature on H16 shows the organism contains two closely related paralogs, norR1 and norR2, each located upstream of a duplicated norAB operon; the proteins are highly similar and (at least partly) functionally redundant. NorR1 is a σ54 (RpoN)-dependent bacterial enhancer-binding protein (bEBP) that senses NO and activates transcription of NO-reduction genes, principally norAB in H16. (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 1-2, busch2004adnaregion pages 1-1, busch2004adnaregion pages 5-6)
NorR1 is not an enzyme; it is a DNA-binding transcriptional activator of the σ54/RpoN family (often grouped with NtrC-like bEBPs). Its core molecular role is to couple an NO-sensing module to ATP-driven remodeling of the σ54-RNA polymerase closed complex, enabling transcription initiation at specific promoters. This definition is supported by genetic evidence in H16 that nor gene transcription requires NorR and RpoN/σ54. (pohlmann2000anovelno‐responding pages 1-2, pohlmann2000anovelno‐responding pages 9-10)
In H16, NorR activates transcription of norAB, where norB encodes a single-subunit qNor-type nitric oxide reductase (NO reductase) and norA encodes a co-transcribed protein of unknown function. Thus, NorR1 sits upstream of a NO-reduction module that lowers intracellular NO burden under oxygen limitation/denitrifying conditions. (busch2004adnaregion pages 1-1, pohlmann2000anovelno‐responding pages 1-2, rodionov2005dissimilatorymetabolismof pages 1-2)
Comparative reconstruction of nitrogen-oxide transcription networks further places NorR among NO-responsive regulators that control NO-reductase genes across proteobacteria (e.g., norVW in E. coli; norAB in R. eutropha/H16), emphasizing that the regulated operon is species-specific—for C. necator H16 the validated target is norAB. (rodionov2005dissimilatorymetabolismof pages 1-2, busch2004adnaregion pages 5-6)
NorR1 in H16 has the “typical modular structure” of σ54 activators:
- N-terminal signaling domain containing a GAF module (the NO-sensing/regulatory component) (busch2004adnaregion pages 1-1, pohlmann2000anovelno‐responding pages 3-4)
- Central AAA+ ATPase/activation domain with conserved nucleotide-binding motifs (pohlmann2000anovelno‐responding pages 2-2)
- C-terminal DNA-binding domain (helix–turn–helix-like) that recognizes enhancer-like upstream binding sites (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 3-4)
This modular architecture aligns with the UniProt/InterPro domain calls supplied in the task prompt (GAF + AAA+_ATPase + DNA-binding). The key functional implication is that NorR1 is expected to be a cytoplasmic protein that binds DNA and interacts with cytoplasmic RNAP–σ54 (i.e., it is not membrane-localized). (pohlmann2000anovelno‐responding pages 1-2, bush2015thestructuralbasis pages 1-3)
Targeted literature searches did not retrieve 2023–2024 primary publications that directly characterize NorR1 (Q9K4V0/PHG246) in C. necator H16. Consequently, the most authoritative organism-specific evidence remains earlier mechanistic genetics/biochemistry from H16 (2000; 2004), complemented by later high-resolution mechanistic/structural work on NorR as a conserved bEBP (2015) and general bEBP/σ54 reviews (2020). (pohlmann2000anovelno‐responding pages 1-2, busch2004adnaregion pages 1-1, bush2015thestructuralbasis pages 1-3, gao2020bacterialenhancerbinding pages 6-8)
Although not 2023–2024, the structural biology work establishing how full-length NorR assembles on enhancer DNA and how the regulatory GAF domain gates ATPase function represents the key “modern” mechanistic framework used for annotation and remains current. In particular, Bush et al. (2015) provided structural and functional characterization of full-length NorR bound to enhancer DNA, refining how signal-dependent conformational changes expose the AAA+ loops required to engage σ54-RNAP. (bush2015thestructuralbasis pages 1-3, bush2015thestructuralbasis pages 10-11)
Directly supported target operons in H16:
- norAB (dicistronic) is activated by NorR in response to NO/NO-generating agents. In the H16 system, authors note norA/norB are the only NorR targets identified in that organism (as of their study). (busch2004adnaregion pages 5-6, busch2004adnaregion pages 1-1)
Gene duplication and redundancy:
- H16 contains two norR genes (norR1 and norR2) upstream of duplicated norAB operons; the NorR proteins are described as duplicated and isofunctional in NO metabolism, and a deletion of megaplasmid-borne norR1 can show little phenotype due to redundancy with norR2. (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 1-2)
NorR binds upstream of the σ54-dependent promoter and recognizes an enhancer region with three conserved inverted repeats. DNase I footprinting defined a 73-bp protected segment containing the NorR boxes; the conserved motif is reported as GGT-(N7)-ACC. Mutations altering the repeats/spacings drastically reduce NorR-dependent activation (reported ~80–90% reduction). (busch2004adnaregion pages 1-1)
These data support annotation of NorR1 as a sequence-specific enhancer-binding transcriptional activator and indicate that promoter activation in H16 depends on a multi-site enhancer architecture. (busch2004adnaregion pages 1-1)
Genetic reporter assays in H16 support NO as the major effector signal for NorR-dependent activation. For example, the NO donor sodium nitroprusside (SNP) restored activity to ~87% of wild-type in a norA-lacZ reporter context, supporting NO as the physiologically relevant activating signal. (pohlmann2000anovelno‐responding pages 6-6)
Deletion/truncation analyses in H16 are consistent with an autoinhibited regulatory model:
- Removing the N-terminal A domain (including the GAF motif) yields a constitutively active NorR derivative, implying that the GAF-containing region normally represses activation in the absence of signal. (pohlmann2000anovelno‐responding pages 6-6)
- Removing additional downstream functional regions abolishes activation, supporting that the central and C-terminal modules are required for transcriptional activation and DNA binding. (pohlmann2000anovelno‐responding pages 6-6)
A modern mechanistic picture comes from full-length NorR structural/functional work:
- NorR is described as a NO-responsive bEBP comprised of an N-terminal GAF domain, central AAA ATPase, and C-terminal DNA-binding domain. NO binds the GAF iron center, forming a mononitrosyl complex that relieves repression of the AAA+ activation machinery; deleting the GAF makes NorR constitutively active. (bush2015thestructuralbasis pages 1-3)
- Enhancer DNA binding stabilizes oligomerization into a higher-mass species (gel filtration shift from 16.5 mL to ~9 mL when DNA is present), and EM supports formation of ring-like oligomers consistent with a hexameric AAA+ ring. (bush2015thestructuralbasis pages 3-5, bush2015thestructuralbasis pages 7-9)
- Structural modeling places GAF domains at the periphery of the AAA ring in the activated state and proposes repression operates by restraining the L1/L2 loops (which include the GAFTGA family motif) that must engage σ54-RNAP; NO-dependent rearrangement exposes these loops for productive σ54 contact and ATP hydrolysis. (bush2015thestructuralbasis pages 10-11, bush2015thestructuralbasis pages 9-10)
Quantitative/structural parameters reported include an EM reconstruction at ~22 Å, an AAA ring diameter around ~155 Å, and a geometric estimate that ~350 Å (~100 bp) of DNA is needed to encircle the hexameric assembly (where a 66 bp fragment is insufficient for stabilization in a tested context). (bush2015thestructuralbasis pages 7-9, bush2015thestructuralbasis pages 9-10)
A detailed mechanistic review of bEBPs summarizes how AAA+ ATP hydrolysis drives conversion of σ54-RNAP closed complexes to open complexes through intermediate states with partial DNA melting (~5–6 bp), DNA kinking (~30°), and formation of a transcription bubble (~13 nt, −11 to +2). While this is not NorR1-specific data, it provides authoritative mechanistic grounding for functional annotation of NorR-family activators (including NorR1) as AAA+ ATPases that remodel RNAP–σ54. (gao2020bacterialenhancerbinding pages 6-8)
Direct localization experiments for H16 NorR1 were not found in the retrieved sources. However, the demonstrated activities—DNA binding upstream of promoters and ATPase-driven interaction with σ54-RNAP—are consistent with NorR1 acting as a cytoplasmic transcription factor associated with the nucleoid (bacterial chromosome/plasmid DNA). No evidence supports membrane or periplasmic localization. (pohlmann2000anovelno‐responding pages 1-2, bush2015thestructuralbasis pages 1-3)
Supported processes for NorR1 in H16:
- Regulation of nitric oxide reduction / NO detoxification under oxygen limitation/denitrifying conditions via activation of norAB. (pohlmann2000anovelno‐responding pages 1-2, busch2004adnaregion pages 1-1)
Although NorR1 itself is a regulatory protein rather than a direct biocatalyst used in industry, its function is relevant to applied use of C. necator H16 because NO/denitrification modules influence redox balance and growth under oxygen-limited conditions.
C. necator H16 is widely used/studied as a biotechnology chassis for hydrogen metabolism and bioenergy applications. In a heterotrophic diauxic batch culture study designed to express soluble hydrogenase (an enzyme of interest for biochemical hydrogen fuel cells), transcriptome-scale changes were measured and provide quantitative context for the organism’s regulated respiratory metabolism:
- qRT-PCR: hoxF ~4.6-fold, hypF2 ~2.2–2.5-fold, hoxA ~4.4–4.5-fold during the derepression/shift conditions. (jugder2015ananalysisof pages 2-4, jugder2015ananalysisof pages 1-2)
- Growth rate changed from ~0.31 h−1 (fructose) to ~0.18 h−1 (glycerol) in the reported system, consistent with an altered energy state that can intersect with respiratory regulation. (jugder2015ananalysisof pages 2-4, jugder2015ananalysisof pages 1-2)
- RNA-seq scale: ~23.2M to ~33.8M read pairs with 98.9–99.15% alignment, and thousands of differentially expressed genes, underscoring the organism’s metabolic plasticity. (jugder2015ananalysisof pages 2-4)
While these data do not directly measure NorR1, they demonstrate the real-world relevance of regulatory networks controlling redox/respiration (including nitrogen-oxide metabolism on megaplasmid pHG1) in bioprocess settings. (jugder2015ananalysisof pages 10-11, jugder2015ananalysisof pages 7-9)
Key quantitative findings useful for functional annotation and promoter engineering:
- NorR1/NorR2 sizes: 513 aa / 521 aa; ~86% identity between paralogs. (pohlmann2000anovelno‐responding pages 2-2)
- NorR boxes in H16 norAB enhancer: 73 bp footprint; motif GGT-(N7)-ACC; motif perturbations reduce activation by ~80–90%. (busch2004adnaregion pages 1-1)
- NO donor effect: SNP restored reporter activity to ~87% of wild type in a norA-lacZ assay context (supporting NO as primary effector). (pohlmann2000anovelno‐responding pages 6-6)
- Structural/biophysical parameters for NorR family: EM reconstruction ~22 Å, model correlation improvement 0.44 → 0.70, gel filtration shift 16.5 mL → ~9 mL with enhancer DNA, estimated ~350 Å (~100 bp) DNA required to encircle hexamer. (bush2015thestructuralbasis pages 10-11, bush2015thestructuralbasis pages 3-5, bush2015thestructuralbasis pages 9-10)
Across organism-specific genetics (H16) and broader mechanistic work (structural NorR, bEBP reviews), NorR1 is best annotated as a dedicated NO-sensing bEBP that activates σ54-dependent transcription of NO-reduction genes. The most defensible, evidence-based “primary function” assignment for Q9K4V0/PHG246 is therefore:
- Molecular function: NO-responsive transcriptional activator (σ54-dependent bEBP)
- Biological process: transcriptional regulation of nitric oxide reduction / nitrosative stress response
- Pathway: NO detoxification branch of denitrification (via norAB activation)
- Cellular location: cytoplasm/nucleoid-associated regulator
This interpretation is directly supported for H16 by the norR1/norR2 duplication and norAB regulation studies, and mechanistically supported by structural work showing how GAF-mediated allostery gates AAA+ ATPase function and σ54 engagement. (pohlmann2000anovelno‐responding pages 1-2, busch2004adnaregion pages 1-1, bush2015thestructuralbasis pages 1-3, bush2015thestructuralbasis pages 10-11)
| Feature | Evidence / Key finding | Organism / system | Quantitative details if any | Primary citation |
|---|---|---|---|---|
| Target identity / disambiguation | UniProt Q9K4V0 corresponds to NorR1, an NO-responsive, σ54/RpoN-dependent transcriptional activator adjacent to a duplicated norAB locus in Cupriavidus necator H16 (syn. Ralstonia eutropha H16). The organism carries two NorR paralogs, NorR1 and NorR2, which are highly similar and functionally redundant in NO metabolism; this matches the UniProt description and warns against confusing it with NorR proteins from other bacteria. | C. necator H16 / R. eutropha H16 | NorR1 513 aa; NorR2 521 aa; ~86% identity between paralogs | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 1-2) |
| Genomic context | norR1 is located upstream of norA1B1 on megaplasmid pHG1; norR2 is upstream of norA2B2 on chromosome II. The denitrification / anaerobiosis context on pHG1 is relevant for annotation of PHG246. | C. necator H16 | Two duplicated norRAB loci; pHG1 encodes key anaerobic / lithoautotrophic functions | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Jugder et al., 2015, https://doi.org/10.1186/s12934-015-0226-4 (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 1-2, jugder2015ananalysisof pages 10-11) |
| Primary molecular function | NorR1 is not an enzyme or transporter; it is a bacterial enhancer-binding protein (bEBP) that activates transcription of NO-detoxification genes by coupling signal sensing to ATP-dependent activation of σ54-RNA polymerase. | NorR family / C. necator H16 | Requires ATP hydrolysis by AAA+ domain for transcriptional activation | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Gao et al., 2020, https://doi.org/10.3390/biom10030351 (pohlmann2000anovelno‐responding pages 9-10, gao2020bacterialenhancerbinding pages 6-8) |
| Domain architecture | NorR1 has the classic modular architecture of a σ54 activator: N-terminal GAF signaling domain, central AAA+ ATPase / activation domain, and C-terminal DNA-binding domain (HTH-like). This agrees with the UniProt / InterPro domain assignment. | C. necator H16 and NorR family | Domain mapping by truncation and sequence analysis; GAF-containing A domain relieves repression when removed | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Büsch et al., 2004, https://doi.org/10.1128/JB.186.23.7980-7987.2004 (pohlmann2000anovelno‐responding pages 2-2, pohlmann2000anovelno‐responding pages 3-4, busch2004adnaregion pages 1-1, pohlmann2000anovelno‐responding pages 6-6) |
| Effector / signal | The physiological effector is nitric oxide (NO). NO or NO-generating compounds induce NorR-dependent promoter activation; the GAF domain is the sensor module. | C. necator H16; NorR family | SNP (NO donor) restored promoter activity to about 87% of wild type in reporter assays; in Bush et al. in vivo assays used 4 mM potassium nitrite as NO-generating condition | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Bush et al., 2015, https://doi.org/10.1111/mmi.12844 (pohlmann2000anovelno‐responding pages 6-6, bush2015thestructuralbasis pages 3-5, bush2015thestructuralbasis pages 1-3) |
| Regulated genes in C. necator | The experimentally identified direct NorR targets in C. necator H16 are norA and norB in the norAB operon; norB encodes a single-subunit qNor-type nitric oxide reductase, while norA encodes a protein of unknown function. | C. necator H16 | Büsch et al. state norA/norB are the only identified NorR targets in this organism | Büsch et al., 2004, https://doi.org/10.1128/JB.186.23.7980-7987.2004; Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x (busch2004adnaregion pages 1-1, busch2004adnaregion pages 5-6, pohlmann2000anovelno‐responding pages 1-2) |
| Cross-species regulon context | Comparative genomics shows NorR regulons in proteobacteria often control NO detoxification genes, including norAB in R. eutropha and norVW in E. coli; however, for this target protein, evidence supports norAB, not norVW, in C. necator. | β- and γ-proteobacteria | Conserved upstream motif linked to norB, norV, hmp, hcp in different species | Rodionov et al., 2005, https://doi.org/10.1371/journal.pcbi.0010055; Büsch et al., 2004, https://doi.org/10.1128/JB.186.23.7980-7987.2004 (rodionov2005dissimilatorymetabolismof pages 1-2, busch2004adnaregion pages 1-1, busch2004adnaregion pages 5-6) |
| DNA-binding site / enhancer architecture | NorR binds a 73-bp protected region upstream of norAB containing three conserved inverted repeats that function as enhancer sites. These are essential for activation. | C. necator H16 | Footprint length 73 bp; motif GGT-(N7)-ACC; mutation of repeats reduced activation by about 80–90% | Büsch et al., 2004, https://doi.org/10.1128/JB.186.23.7980-7987.2004 (busch2004adnaregion pages 1-1) |
| σ54 dependence | NorR works through a σ54-dependent promoter upstream of norAB; NorR and RpoN are both required for norB1 expression. | C. necator H16 | Functional dependence demonstrated with promoter fusions / mutant analysis | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Büsch et al., 2004, https://doi.org/10.1128/JB.186.23.7980-7987.2004 (pohlmann2000anovelno‐responding pages 1-2, pohlmann2000anovelno‐responding pages 9-10, busch2004adnaregion pages 5-6) |
| Mechanism of repression and activation | The GAF domain represses the AAA+ transcription-activation machinery in the absence of NO. Removal of the GAF-containing A domain makes NorR constitutively active, showing intramolecular negative control. | C. necator H16; NorR family | ΔA/GAF mutant constitutive; deletions removing additional downstream regions abolish activation | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x (pohlmann2000anovelno‐responding pages 6-6, pohlmann2000anovelno‐responding pages 9-10) |
| Structural activation model | Enhancer DNA binding promotes assembly of NorR into a hexameric AAA+ ring. NO signaling causes the GAF domains to move to the periphery, exposing L1/L2 loops (with the GAFTGA motif in the family) so the ATPase ring can engage σ54-RNAP and remodel the closed complex into an open complex. | NorR model system / family-level inference applicable to NorR1 | EM reconstruction at ~22 Å; map filtered to ~28 Å; model correlation improved 0.44 → 0.70 | Bush et al., 2015, https://doi.org/10.1111/mmi.12844; Gao et al., 2020, https://doi.org/10.3390/biom10030351 (bush2015thestructuralbasis pages 10-11, bush2015thestructuralbasis pages 7-9, bush2015thestructuralbasis pages 1-3, bush2015thestructuralbasis pages 9-10, gao2020bacterialenhancerbinding pages 6-8) |
| Oligomerization and enhancer dependence | NorR is unusual among bEBPs in requiring three enhancer sites; binding enhancer DNA stabilizes higher-order oligomers even before activation. | NorR model system / family-level inference | Gel filtration shift from 16.5 mL monomer to ~9 mL high-mass species on DNA; ~100 bp / ~350 Å DNA estimated to encircle hexamer; 66 bp insufficient | Bush et al., 2015, https://doi.org/10.1111/mmi.12844 (bush2015thestructuralbasis pages 3-5, bush2015thestructuralbasis pages 1-3, bush2015thestructuralbasis pages 9-10) |
| ATPase-coupled transcription activation | Like other bEBPs, NorR uses ATP hydrolysis in an AAA+ hexamer to remodel σ54-RNAP. General bEBP structural work explains how ATPase-driven L1/L2 loop movements promote DNA opening and transcription initiation. | bEBP / σ54 field | Structural snapshots in bEBP field: partial melting 5–6 bp, DNA kink ~30°, transcription bubble 13 nt | Gao et al., 2020, https://doi.org/10.3390/biom10030351 (gao2020bacterialenhancerbinding pages 6-8) |
| Activated mutant evidence | A Q304E substitution in NorR partially bypasses GAF repression, producing enhancer-independent ATPase activity and NO-independent transcription in vivo, supporting the allosteric model. | NorR model system / family-level inference | Q304E active without added NO; Walker B D286A suppresses ATPase activity | Bush et al., 2015, https://doi.org/10.1111/mmi.12844 (bush2015thestructuralbasis pages 3-5, bush2015thestructuralbasis pages 7-9, bush2015thestructuralbasis pages 9-10) |
| Localization | NorR1 is a soluble cytoplasmic DNA-binding transcription factor acting at the cytoplasmic face of chromosomal / plasmid DNA and interacting with cytoplasmic σ54-RNAP; it is not a membrane or periplasmic protein. | Inference from function/domain architecture | No transmembrane role reported; acts on upstream enhancer DNA of norAB | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Bush et al., 2015, https://doi.org/10.1111/mmi.12844 (pohlmann2000anovelno‐responding pages 1-2, bush2015thestructuralbasis pages 1-3) |
| Biological pathway | NorR1 functions in the nitrosative stress / NO detoxification branch of denitrification, activating expression of nitric oxide reductase so NO can be reduced under low-oxygen / denitrifying conditions. | C. necator H16 and broader nitrogen-oxide metabolism | Reporter induction observed under anoxia / denitrification conditions | Pohlmann et al., 2000, https://doi.org/10.1046/j.1365-2958.2000.02157.x; Rodionov et al., 2005, https://doi.org/10.1371/journal.pcbi.0010055 (pohlmann2000anovelno‐responding pages 1-2, pohlmann2000anovelno‐responding pages 9-10, rodionov2005dissimilatorymetabolismof pages 1-2) |
| Organism-level application context | C. necator H16 is industrially relevant for hydrogenase-based bioenergy, electrocatalysis, CO2-fixing lithoautotrophy, and PHA bioplastic production. These applications make respiratory and redox regulators, including NO/denitrification modules on pHG1, relevant for process optimization under oxygen-limited conditions. | C. necator H16 biotechnology | hoxF up 4.6-fold, hypF2 2.2–2.5-fold, hoxA ~4.4–4.5-fold; growth rate 0.31 h−1 on fructose vs 0.18 h−1 on glycerol; RNA-seq alignment 98.9–99.15% | Jugder et al., 2015, https://doi.org/10.1186/s12934-015-0226-4 (jugder2015ananalysisof pages 2-4, jugder2015ananalysisof pages 1-2, jugder2015ananalysisof pages 7-9) |
Table: This table summarizes the verified identity, domain architecture, molecular mechanism, regulon, and biological context of Cupriavidus necator H16 NorR1 (UniProt Q9K4V0). It highlights which findings are directly organism-specific versus inferred from closely studied NorR-family structural work.
References
(pohlmann2000anovelno‐responding pages 2-2): Anne Pohlmann, Rainer Cramm, Karin Schmelz, and Bärbel Friedrich. A novel no‐responding regulator controls the reduction of nitric oxide in ralstonia eutropha. Molecular Microbiology, 38:626-638, Nov 2000. URL: https://doi.org/10.1046/j.1365-2958.2000.02157.x, doi:10.1046/j.1365-2958.2000.02157.x. This article has 142 citations and is from a domain leading peer-reviewed journal.
(pohlmann2000anovelno‐responding pages 1-2): Anne Pohlmann, Rainer Cramm, Karin Schmelz, and Bärbel Friedrich. A novel no‐responding regulator controls the reduction of nitric oxide in ralstonia eutropha. Molecular Microbiology, 38:626-638, Nov 2000. URL: https://doi.org/10.1046/j.1365-2958.2000.02157.x, doi:10.1046/j.1365-2958.2000.02157.x. This article has 142 citations and is from a domain leading peer-reviewed journal.
(busch2004adnaregion pages 1-1): Andrea Büsch, Anne Pohlmann, Bärbel Friedrich, and Rainer Cramm. A dna region recognized by the nitric oxide-responsive transcriptional activator norr is conserved in β- and γ-proteobacteria. Journal of Bacteriology, 186:7980-7987, Dec 2004. URL: https://doi.org/10.1128/jb.186.23.7980-7987.2004, doi:10.1128/jb.186.23.7980-7987.2004. This article has 29 citations and is from a peer-reviewed journal.
(busch2004adnaregion pages 5-6): Andrea Büsch, Anne Pohlmann, Bärbel Friedrich, and Rainer Cramm. A dna region recognized by the nitric oxide-responsive transcriptional activator norr is conserved in β- and γ-proteobacteria. Journal of Bacteriology, 186:7980-7987, Dec 2004. URL: https://doi.org/10.1128/jb.186.23.7980-7987.2004, doi:10.1128/jb.186.23.7980-7987.2004. This article has 29 citations and is from a peer-reviewed journal.
(pohlmann2000anovelno‐responding pages 9-10): Anne Pohlmann, Rainer Cramm, Karin Schmelz, and Bärbel Friedrich. A novel no‐responding regulator controls the reduction of nitric oxide in ralstonia eutropha. Molecular Microbiology, 38:626-638, Nov 2000. URL: https://doi.org/10.1046/j.1365-2958.2000.02157.x, doi:10.1046/j.1365-2958.2000.02157.x. This article has 142 citations and is from a domain leading peer-reviewed journal.
(rodionov2005dissimilatorymetabolismof pages 1-2): Dmitry A Rodionov, Inna L Dubchak, Adam P Arkin, Eric J Alm, and Mikhail S Gelfand. Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks. PLoS Computational Biology, 1:e55, Sep 2005. URL: https://doi.org/10.1371/journal.pcbi.0010055, doi:10.1371/journal.pcbi.0010055. This article has 358 citations and is from a highest quality peer-reviewed journal.
(pohlmann2000anovelno‐responding pages 3-4): Anne Pohlmann, Rainer Cramm, Karin Schmelz, and Bärbel Friedrich. A novel no‐responding regulator controls the reduction of nitric oxide in ralstonia eutropha. Molecular Microbiology, 38:626-638, Nov 2000. URL: https://doi.org/10.1046/j.1365-2958.2000.02157.x, doi:10.1046/j.1365-2958.2000.02157.x. This article has 142 citations and is from a domain leading peer-reviewed journal.
(bush2015thestructuralbasis pages 1-3): Matt Bush, Tamaswati Ghosh, Marta Sawicka, Iain H. Moal, Paul A. Bates, Ray Dixon, and Xiaodong Zhang. The structural basis for enhancer‐dependent assembly and activation of the aaa transcriptional activator norr. Molecular Microbiology, 95:17-30, Jan 2015. URL: https://doi.org/10.1111/mmi.12844, doi:10.1111/mmi.12844. This article has 21 citations and is from a domain leading peer-reviewed journal.
(gao2020bacterialenhancerbinding pages 6-8): Forson Gao, Amy E. Danson, Fuzhou Ye, Milija Jovanovic, Martin Buck, and Xiaodong Zhang. Bacterial enhancer binding proteins—aaa+ proteins in transcription activation. Biomolecules, 10:351, Feb 2020. URL: https://doi.org/10.3390/biom10030351, doi:10.3390/biom10030351. This article has 43 citations.
(bush2015thestructuralbasis pages 10-11): Matt Bush, Tamaswati Ghosh, Marta Sawicka, Iain H. Moal, Paul A. Bates, Ray Dixon, and Xiaodong Zhang. The structural basis for enhancer‐dependent assembly and activation of the aaa transcriptional activator norr. Molecular Microbiology, 95:17-30, Jan 2015. URL: https://doi.org/10.1111/mmi.12844, doi:10.1111/mmi.12844. This article has 21 citations and is from a domain leading peer-reviewed journal.
(pohlmann2000anovelno‐responding pages 6-6): Anne Pohlmann, Rainer Cramm, Karin Schmelz, and Bärbel Friedrich. A novel no‐responding regulator controls the reduction of nitric oxide in ralstonia eutropha. Molecular Microbiology, 38:626-638, Nov 2000. URL: https://doi.org/10.1046/j.1365-2958.2000.02157.x, doi:10.1046/j.1365-2958.2000.02157.x. This article has 142 citations and is from a domain leading peer-reviewed journal.
(bush2015thestructuralbasis pages 3-5): Matt Bush, Tamaswati Ghosh, Marta Sawicka, Iain H. Moal, Paul A. Bates, Ray Dixon, and Xiaodong Zhang. The structural basis for enhancer‐dependent assembly and activation of the aaa transcriptional activator norr. Molecular Microbiology, 95:17-30, Jan 2015. URL: https://doi.org/10.1111/mmi.12844, doi:10.1111/mmi.12844. This article has 21 citations and is from a domain leading peer-reviewed journal.
(bush2015thestructuralbasis pages 7-9): Matt Bush, Tamaswati Ghosh, Marta Sawicka, Iain H. Moal, Paul A. Bates, Ray Dixon, and Xiaodong Zhang. The structural basis for enhancer‐dependent assembly and activation of the aaa transcriptional activator norr. Molecular Microbiology, 95:17-30, Jan 2015. URL: https://doi.org/10.1111/mmi.12844, doi:10.1111/mmi.12844. This article has 21 citations and is from a domain leading peer-reviewed journal.
(bush2015thestructuralbasis pages 9-10): Matt Bush, Tamaswati Ghosh, Marta Sawicka, Iain H. Moal, Paul A. Bates, Ray Dixon, and Xiaodong Zhang. The structural basis for enhancer‐dependent assembly and activation of the aaa transcriptional activator norr. Molecular Microbiology, 95:17-30, Jan 2015. URL: https://doi.org/10.1111/mmi.12844, doi:10.1111/mmi.12844. This article has 21 citations and is from a domain leading peer-reviewed journal.
(jugder2015ananalysisof pages 2-4): Bat-Erdene Jugder, Zhiliang Chen, Darren Tan Tek Ping, Helene Lebhar, Jeffrey Welch, and Christopher P Marquis. An analysis of the changes in soluble hydrogenase and global gene expression in cupriavidus necator (ralstonia eutropha) h16 grown in heterotrophic diauxic batch culture. Microbial Cell Factories, Mar 2015. URL: https://doi.org/10.1186/s12934-015-0226-4, doi:10.1186/s12934-015-0226-4. This article has 49 citations and is from a peer-reviewed journal.
(jugder2015ananalysisof pages 1-2): Bat-Erdene Jugder, Zhiliang Chen, Darren Tan Tek Ping, Helene Lebhar, Jeffrey Welch, and Christopher P Marquis. An analysis of the changes in soluble hydrogenase and global gene expression in cupriavidus necator (ralstonia eutropha) h16 grown in heterotrophic diauxic batch culture. Microbial Cell Factories, Mar 2015. URL: https://doi.org/10.1186/s12934-015-0226-4, doi:10.1186/s12934-015-0226-4. This article has 49 citations and is from a peer-reviewed journal.
(jugder2015ananalysisof pages 10-11): Bat-Erdene Jugder, Zhiliang Chen, Darren Tan Tek Ping, Helene Lebhar, Jeffrey Welch, and Christopher P Marquis. An analysis of the changes in soluble hydrogenase and global gene expression in cupriavidus necator (ralstonia eutropha) h16 grown in heterotrophic diauxic batch culture. Microbial Cell Factories, Mar 2015. URL: https://doi.org/10.1186/s12934-015-0226-4, doi:10.1186/s12934-015-0226-4. This article has 49 citations and is from a peer-reviewed journal.
(jugder2015ananalysisof pages 7-9): Bat-Erdene Jugder, Zhiliang Chen, Darren Tan Tek Ping, Helene Lebhar, Jeffrey Welch, and Christopher P Marquis. An analysis of the changes in soluble hydrogenase and global gene expression in cupriavidus necator (ralstonia eutropha) h16 grown in heterotrophic diauxic batch culture. Microbial Cell Factories, Mar 2015. URL: https://doi.org/10.1186/s12934-015-0226-4, doi:10.1186/s12934-015-0226-4. This article has 49 citations and is from a peer-reviewed journal.