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The UniProt accession Q88I42 corresponds to BenR, annotated as the “BenABC operon transcriptional activator” from Pseudomonas putida strain KT2440, with ordered locus name PP_3159. A 2023 experimental/synthetic-biology study explicitly identifies P. putida benR as PP_3159 and characterizes benzoate-responsive promoters in this genomic region, confirming that the literature summarized here matches the intended target (Pearson et al., 2023-12, https://doi.org/10.1021/acssynbio.3c00441). (pearson2023characterizationanddiversification pages 5-8)
BenR is a DNA-binding transcriptional regulator in the AraC/XylS family, closely related to the aromatic-response regulator XylS. In P. putida, BenR is described as a XylS homologue (AraC-family) with typical architecture for this family (N-terminal effector/activation region; C-terminal helix-turn-helix DNA-binding domain), and Cowles et al. report BenR as a ~318 aa (~36.4 kDa) regulator. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 6-7)
Functional definition: BenR is best understood as a benzoate-responsive transcriptional activator that turns on expression of genes needed to initiate benzoate catabolism, chiefly the benABC benzoate dioxygenase gene cluster. (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 3-4)
The benzoate (ben) catabolic region contains structural genes encoding the initial oxidation of benzoate (benzoate dioxygenase components BenA/BenB/BenC, with downstream steps including BenD discussed), and nearby genes associated with uptake (e.g., benK transporter; benF porin), consistent with the idea that BenR couples substrate sensing (benzoate presence) to catabolic gene expression. (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 5-6)
BenR functions as an intracellular (cytosolic) DNA-binding transcription factor, acting at chromosomal promoters (e.g., the benA/Pben promoter region) and capable of acting at related promoters in heterologous hosts when expressed there. This is supported by (i) its AraC/XylS-family identity, and (ii) extensive promoter-reporter and cross-promoter activation assays performed in Pseudomonas and E. coli. (cowles2000benraxyls pages 3-4, cowles2000benraxyls pages 7-8)
Key experimental evidence (genetics + reporter assays):
* Cowles et al. constructed a benA promoter–lacZ transcriptional fusion and found that adding benzoate increased reporter activity by about ~15-fold in wild-type P. putida, while catechol did not induce the fusion. A benR mutant failed to induce the benA reporter in response to benzoate, demonstrating BenR is required for benzoate-dependent activation of benA/benABC. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 3-4)
* RT-PCR evidence indicates benA, benB, benC are cotranscribed in benzoate-grown cells, consistent with BenR controlling an operon-level response. (cowles2000benraxyls pages 4-5)
Interpretation: These experiments establish BenR as the primary on-switch for the benzoate entry pathway in P. putida, rather than a downstream metabolite (catechol) sensor. (cowles2000benraxyls pages 3-4)
Cowles et al. provide evidence consistent with direct transcriptional activation: when BenR was overexpressed in E. coli carrying a benA-lacZ reporter, reporter expression rose by ~25-fold compared with no benR. In this high-expression context, adding benzoate did not further increase expression, implying that BenR can become effectively constitutively activating when abundant (a behavior commonly observed for AraC-family activators in heterologous or overexpression contexts). (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 3-4)
Cowles et al. mapped the benA transcription start site by primer extension, placing the 5′ end ~30 bp upstream of the predicted start, and note direct-repeat elements in the ben promoter region consistent with operator architectures described for XylS-family regulators. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 7-8)
Pérez-Pantoja et al. additionally provide a promoter map depiction of conserved distal/proximal operator-like boxes and core promoter elements for Pben in P. putida mt-2, which is useful for engineering and for conceptualizing BenR binding/activation logic at Pben. (Pérez-Pantoja et al., 2015-04, https://doi.org/10.1111/1462-2920.12443). (perez‐pantoja2015thedifferentialresponse pages 23-26)
A benR null mutant is defective for growth on benzoate, and plasmid-borne benR complements this phenotype. Cowles et al. report that the complemented strain grows on benzoate with a generation time of ~2.4 h vs ~1.8 h for wild type, supporting BenR as a key determinant of efficient benzoate utilization. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 4-5)
Cowles et al. show BenR is involved in benzoate-mediated repression of pcaK, a 4-hydroxybenzoate (4-HBA) uptake system. In wild-type cells, growth on benzoate + 4-HBA reduces pcaK promoter reporter activity ~5-fold relative to 4-HBA alone. Physiologically, 4-HBA uptake was ~10-fold lower when wild type was grown on benzoate + 4-HBA versus 4-HBA alone, while a benR mutant retained high uptake (~25 nmol·min⁻¹·mg⁻¹). (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 6-7, cowles2000benraxyls pages 5-6)
Interpretation: Beyond activating benzoate catabolism, BenR participates in prioritization/coordination among aromatic carbon sources, plausibly reducing metabolic conflict by down-modulating 4-HBA uptake when benzoate is present. (cowles2000benraxyls pages 6-7)
Cowles et al. show that BenR can activate the TOL plasmid Pm promoter in E. coli, reaching ~13,000 Miller units (with a modest increase to ~17,000 with benzoate in one setup), indicating potential cross-regulation among XylS/BenR-family promoters. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 4-5)
Pérez-Pantoja et al. (2015) systematically tested Pben regulation in P. putida using chromosomally integrated lux reporters. They conclude that BenR is necessary for strong induction of Pben by benzoate and that physiological levels of the alternative regulator XylS do not significantly activate Pben. Only artificially high XylS overexpression yields measurable Pben activity, and even then Pben responses are ~10–15-fold weaker than XylS activation of Pm. (Pérez-Pantoja et al., 2015-04, https://doi.org/10.1111/1462-2920.12443). (perez‐pantoja2015thedifferentialresponse pages 7-9)
Image-supported evidence: The figures retrieved from Pérez-Pantoja et al. show strong Pben induction by benzoate in benR+ backgrounds and near-silence of Pben in benR mutants unless XylS is overproduced. (perez‐pantoja2015thedifferentialresponse media 32f9b80f, perez‐pantoja2015thedifferentialresponse media 92d90004)
Pearson et al. (2023-12, ACS Synthetic Biology; https://doi.org/10.1021/acssynbio.3c00441) evaluated promoter fragments near PP_3159 (benR) in P. putida and found a strong benzoate-inducible promoter upstream of PP_3161 with 38 ± 5.2-fold induction at 10 mM benzoate, while a promoter upstream of PP_3160 showed only 1.7 ± 0.20-fold induction. They also note that benzoate induction was hampered at 20 mM due to toxicity. (pearson2023characterizationanddiversification pages 5-8)
Expert analysis: This type of measured fold-induction under defined inducer concentrations provides “parts-grade” quantitative data supporting BenR/Pben as a robust inducible module and clarifies that promoter choice within the ben locus (PP_3161 vs PP_3160 upstream regions) strongly affects dynamic range. (pearson2023characterizationanddiversification pages 5-8)
Hanko et al. (2023-04, ACS Synthetic Biology; https://doi.org/10.1021/acssynbio.2c00679) use BenR as an explicit example of a known benzoate-responsive transcription factor adjacent to the benzoate catabolic operon in P. putida, and report that their TFBMiner pipeline did not recover P. putida BenR because benR is encoded on the same strand as the catabolic operon (a limitation of their gene-organization heuristic), even though the enzymatic chain was predicted. (hanko2023tfbminerauserfriendly pages 6-7)
Expert analysis: This highlights a practical annotation pitfall: operon orientation and database constraints can cause automated pipelines to miss biologically correct regulators, so BenR is a useful “ground truth” control for functional annotation workflows. (hanko2023tfbminerauserfriendly pages 6-7)
A 2024 ACS Synthetic Biology review on regulatory components for bacterial cell-free systems lists BenR/Pben as an example in which benzoic acid activates BenR, which then activates Pben, illustrating how native bacterial regulators are repurposed for cell-free circuit design. (Lee & Maerkl, 2024-11, https://doi.org/10.1021/acssynbio.4c00574). (perez‐pantoja2015thedifferentialresponse pages 23-26)
Note: The retrieved excerpt provides contextual mention rather than detailed performance metrics. (perez‐pantoja2015thedifferentialresponse pages 23-26)
BenR/Pben has been engineered into chromosomal lux reporters in Pseudomonas to provide stable, low-copy, quantitative readouts of benzoate-responsive transcription—useful in pathway debugging, environmental sensing, and managing regulatory cross-talk in aromatic-degradation chassis. (Pérez-Pantoja et al., 2015-04, https://doi.org/10.1111/1462-2920.12443). (perez‐pantoja2015thedifferentialresponse pages 7-9, perez‐pantoja2015thedifferentialresponse media 32f9b80f)
A later review summarizes work (attributed there to Voyvodic et al.) in which BenR/Pben was used in a modular cell-free biosensor design; the review reports benzoate detection in commercial beverages with signal fold-changes up to ~180-fold, and extension to detect other analytes (e.g., hippuric acid and cocaine-related targets) via upstream enzymatic conversion modules. (Dou et al., 2025-12, https://doi.org/10.1186/s44314-025-00032-7). (dou2025detectionofenvironmental pages 7-10)
Interpretation: While this is a secondary-source summary (not a 2023–2024 primary paper), it indicates a plausible pathway from BenR’s native function to deployable sensing in complex matrices (beverages; urine). (dou2025detectionofenvironmental pages 7-10)
Key quantitative findings available from primary sources include:
* ~15-fold benA promoter induction by benzoate in wild-type P. putida; no induction by catechol. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 3-4)
* ~25-fold benA promoter activation when BenR is overexpressed in E. coli with benA-lacZ reporter. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 3-4)
* BenR activation of Pm to ~13,000 Miller units (to ~17,000 with benzoate in one setup). (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 4-5)
* Benzoate-mediated repression effects linked to BenR: ~5-fold lower pcaK reporter activity; ~10-fold reduced 4-HBA uptake in wild type on benzoate+4-HBA; benR mutant retains ~25 nmol·min⁻¹·mg⁻¹ uptake. (Cowles et al., 2000-11, https://doi.org/10.1128/jb.182.22.6339-6346.2000). (cowles2000benraxyls pages 6-7, cowles2000benraxyls pages 5-6)
* 2023 “parts-grade” promoter performance near benR: 38 ± 5.2-fold induction for P_PP_3161 at 10 mM benzoate, vs 1.7 ± 0.20 for P_PP_3160; benzoate toxicity noted at 20 mM. (Pearson et al., 2023-12, https://doi.org/10.1021/acssynbio.3c00441). (pearson2023characterizationanddiversification pages 5-8)
BenR (PP_3159; UniProt Q88I42) is best annotated as a benzoate-responsive AraC/XylS-family transcriptional activator that operates in the cytoplasm by binding and activating the benA/Pben promoter and turning on the benABC operon required for initiating benzoate catabolism (benzoate → catechol entry). Genetic loss-of-function, promoter-reporter assays, and complementation show BenR is required for benzoate induction and for efficient growth on benzoate. BenR additionally contributes to aromatic substrate prioritization, participating in benzoate-mediated repression of the pcaK 4-HBA uptake system, and exhibits limited cross-talk potential with the XylS-controlled TOL system, though Pben is largely insulated from XylS under physiological conditions. (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 3-4, cowles2000benraxyls pages 6-7, perez‐pantoja2015thedifferentialresponse pages 7-9)
| Functional aspect | Key findings | Experimental approach/model system | Main citation |
|---|---|---|---|
| Target identity / gene mapping | BenR is the benzoate-responsive AraC/XylS-family transcriptional activator encoded by PP_3159, matching UniProt Q88I42; located adjacent to the benzoate catabolic operon in Pseudomonas putida. | Genomic context analysis, promoter-reporter characterization, comparative annotation in P. putida. | Pearson et al. 2023, ACS Synth Biol, DOI: 10.1021/acssynbio.3c00441, https://doi.org/10.1021/acssynbio.3c00441; Hanko et al. 2023, ACS Synth Biol, DOI: 10.1021/acssynbio.2c00679, https://doi.org/10.1021/acssynbio.2c00679 (pearson2023characterizationanddiversification pages 5-8, hanko2023tfbminerauserfriendly pages 6-7) |
| Regulator family / domains | BenR is a XylS homolog in the AraC/XylS family; sequence analyses place it among regulators with conserved C-terminal HTH DNA-binding motifs, consistent with UniProt domain calls (AraC-bd_2 / HTH_AraC-type architecture). Cowles et al. describe a 318 aa (~36.4 kDa) regulator with strong similarity to XylS. | Sequence comparison, operon cloning, mutational analysis. | Cowles et al. 2000, J Bacteriol, DOI: 10.1128/JB.182.22.6339-6346.2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 6-7) |
| Primary regulated genes / operons | BenR activates the benABC operon (and benzoate locus including benD, with nearby transport-related genes benK/benF/benE discussed in the locus). benA, benB, benC are cotranscribed in benzoate-grown cells. | benA-lacZ reporter assays, RT-PCR, complementation of benR mutant, growth phenotyping on benzoate. | Cowles et al. 2000, J Bacteriol, DOI: 10.1128/JB.182.22.6339-6346.2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 4-5) |
| Inducer / effector specificity | Native BenR responds primarily to benzoate; catechol does not induce benA-lacZ in the native system. In engineered/synthetic contexts, broader responsiveness to 3-methylbenzoate and salicylate was observed for one BenR-derived construct, likely due to altered promoter architecture and/or increased BenR levels. | Native benA-lacZ assays in P. putida; engineered single-plasmid reporter systems in E. coli / P. putida. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000; Pearson et al. 2023, https://doi.org/10.1021/acssynbio.3c00441 (cowles2000benraxyls pages 3-4, pearson2023characterizationanddiversification pages 20-23) |
| Native induction strength | In wild-type P. putida, benzoate increased benA-lacZ ~15-fold versus succinate alone; benR mutants lost this benzoate inducibility. | benA promoter-lacZ reporter in wild type vs benR mutant. | Cowles et al. 2000, J Bacteriol, DOI: 10.1128/JB.182.22.6339-6346.2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 3-4) |
| Direct activation evidence | Overexpression of BenR in E. coli increased benA-lacZ ~25-fold, supporting direct activation of the benA promoter; in that overexpression context, added benzoate did not further increase signal, implying constitutive activation when BenR is highly abundant. | Heterologous T7-driven BenR overexpression in E. coli BL21(DE3) carrying benA-lacZ. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 3-4) |
| Promoter/operator features | Primer extension mapped the benA transcription start ~30 bp upstream of the predicted start codon. The ben promoter region contains direct-repeat elements resembling XylS/BenR-family binding arrangements; one study also notes promoter/operator organization with conserved distal/proximal boxes useful for engineering. | Primer extension, reporter mapping, comparative promoter analysis, engineered lux reporters. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000; Pérez-Pantoja et al. 2015, DOI: 10.1111/1462-2920.12443, https://doi.org/10.1111/1462-2920.12443 (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 7-8, perez‐pantoja2015thedifferentialresponse pages 23-26) |
| Physiological role in benzoate catabolism | benR null mutants are defective for growth on benzoate; complementation with plasmid-borne benR restores growth, with reported generation time ~2.4 h for complemented strain versus ~1.8 h for wild type. BenR therefore functions as the key transcriptional activator enabling benzoate utilization. | benR mutant construction, plasmid complementation, growth assays on benzoate. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 4-5) |
| Additional regulon effects / pathway coordination | BenR also participates in benzoate-mediated repression of the pcaK 4-hydroxybenzoate uptake system, linking benzoate sensing to coordination of aromatic acid catabolism. Growth on benzoate + 4-HBA reduced pcaK-driven reporter activity ~5-fold, and wild-type cells showed ~10-fold lower 4-HBA uptake versus 4-HBA alone; benR mutants retained high uptake (~25 nmol·min⁻¹·mg⁻¹). | pcaK-lacZ reporter assays, uptake assays, benR mutant comparison, heterologous tests for direct regulation. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 6-7, cowles2000benraxyls pages 5-6) |
| Cross-talk with XylS | BenR can activate the TOL plasmid Pm promoter; heterologous assays reported 13,000 Miller units from Pm with BenR, increasing to 17,000 Miller units with benzoate in one setup. Conversely, XylS can only partially substitute for BenR at Pben under some conditions. | Pm-lacZ assays in E. coli; TOL plasmid introduction into benR mutant. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000 (cowles2000benraxyls pages 4-5, cowles2000benraxyls pages 7-8, cowles2000benraxyls pages 3-4) |
| Functional insulation of Pben vs XylS | In P. putida mt-2, physiological XylS levels do not significantly activate Pben; only artificial XylS overexpression gives measurable Pben induction, and even then responses are 10–15-fold weaker than XylS activation of Pm. A benR mutant fails to grow on 5 mM benzoate unless XylS is overexpressed from medium/high-copy plasmids. | Chromosomal Pben::luxCDABE and Pm::luxCDABE reporters, regulator dosage series, benR mutant growth tests. | Pérez-Pantoja et al. 2015, Environ Microbiol, DOI: 10.1111/1462-2920.12443, https://doi.org/10.1111/1462-2920.12443 (perez‐pantoja2015thedifferentialresponse pages 7-9) |
| Quantitative promoter characterization in recent work | In 2023 characterization of PP_3159-associated promoters, P_PP_3161 showed 38 ± 5.2-fold induction at 10 mM benzoate, while P_PP_3160 showed only 1.7 ± 0.20-fold. Induction was hampered at 20 mM benzoate because of toxicity. | 200 bp upstream promoter fragments fused to RFP in P. putida; benzoate dose testing. | Pearson et al. 2023, https://doi.org/10.1021/acssynbio.3c00441 (pearson2023characterizationanddiversification pages 5-8) |
| Biosensor / synthetic biology use | BenR–Pben has been used as a specific benzoate-responsive biosensor module and as a reporter/control pair in synthetic biology. TFBMiner cites BenR as a canonical benzoate-responsive TF adjacent to the benzoate catabolic operon. Reviews and later reports highlight BenR/PBen in modular biosensing, including cell-free benzoate detection workflows. | Biosensor mining pipeline example; reporter engineering; synthetic biology reviews. | Hanko et al. 2023, https://doi.org/10.1021/acssynbio.2c00679; Lee & Maerkl 2024, DOI: 10.1021/acssynbio.4c00574, https://doi.org/10.1021/acssynbio.4c00574 (hanko2023tfbminerauserfriendly pages 6-7) |
| Real-world implementation example | A later review summarizes a cell-free BenR/PBen platform detecting benzoate in beverages with signal changes up to ~180-fold, and modular extensions for detecting metabolites such as hippuric acid and cocaine-derived products via upstream conversion modules. | Cell-free transcription-factor biosensor workflow summarized in review literature. | Dou et al. 2025, https://doi.org/10.1186/s44314-025-00032-7 (reviewed application) (dou2025detectionofenvironmental pages 7-10) |
| Cellular localization / site of action | BenR is a soluble intracellular DNA-binding transcription factor expected to act in the cytoplasm at chromosomal/plasmid promoters rather than as a membrane or secreted protein; this inference is supported by its AraC/XylS-family regulator architecture and promoter-centric experimental evidence. | Domain/family inference plus transcriptional reporter and promoter-binding functional data. | Cowles et al. 2000, https://doi.org/10.1128/jb.182.22.6339-6346.2000; Pearson et al. 2023, https://doi.org/10.1021/acssynbio.3c00441 (cowles2000benraxyls pages 7-8, pearson2023characterizationanddiversification pages 5-8) |
Table: This table summarizes experimentally supported functional annotation for BenR (PP_3159; UniProt Q88I42) in Pseudomonas putida, including regulation, inducer specificity, promoter behavior, physiology, and synthetic biology use. It highlights quantitative metrics and the main papers supporting each annotation point.
References
(pearson2023characterizationanddiversification pages 5-8): Allison N. Pearson, Matthew R. Incha, Cindy N. Ho, Matthias Schmidt, Jacob B. Roberts, Alberto A. Nava, and Jay D. Keasling. Characterization and diversification of arac/xyls family regulators guided by transposon sequencing. ACS Synthetic Biology, 13:206-219, Dec 2023. URL: https://doi.org/10.1021/acssynbio.3c00441, doi:10.1021/acssynbio.3c00441. This article has 5 citations and is from a domain leading peer-reviewed journal.
(cowles2000benraxyls pages 4-5): Charles E. Cowles, Nancy N. Nichols, and Caroline S. Harwood. Benr, a xyls homologue, regulates three different pathways of aromatic acid degradation in pseudomonas putida. Journal of Bacteriology, 182:6339-6346, Nov 2000. URL: https://doi.org/10.1128/jb.182.22.6339-6346.2000, doi:10.1128/jb.182.22.6339-6346.2000. This article has 193 citations and is from a peer-reviewed journal.
(cowles2000benraxyls pages 6-7): Charles E. Cowles, Nancy N. Nichols, and Caroline S. Harwood. Benr, a xyls homologue, regulates three different pathways of aromatic acid degradation in pseudomonas putida. Journal of Bacteriology, 182:6339-6346, Nov 2000. URL: https://doi.org/10.1128/jb.182.22.6339-6346.2000, doi:10.1128/jb.182.22.6339-6346.2000. This article has 193 citations and is from a peer-reviewed journal.
(cowles2000benraxyls pages 3-4): Charles E. Cowles, Nancy N. Nichols, and Caroline S. Harwood. Benr, a xyls homologue, regulates three different pathways of aromatic acid degradation in pseudomonas putida. Journal of Bacteriology, 182:6339-6346, Nov 2000. URL: https://doi.org/10.1128/jb.182.22.6339-6346.2000, doi:10.1128/jb.182.22.6339-6346.2000. This article has 193 citations and is from a peer-reviewed journal.
(cowles2000benraxyls pages 5-6): Charles E. Cowles, Nancy N. Nichols, and Caroline S. Harwood. Benr, a xyls homologue, regulates three different pathways of aromatic acid degradation in pseudomonas putida. Journal of Bacteriology, 182:6339-6346, Nov 2000. URL: https://doi.org/10.1128/jb.182.22.6339-6346.2000, doi:10.1128/jb.182.22.6339-6346.2000. This article has 193 citations and is from a peer-reviewed journal.
(cowles2000benraxyls pages 7-8): Charles E. Cowles, Nancy N. Nichols, and Caroline S. Harwood. Benr, a xyls homologue, regulates three different pathways of aromatic acid degradation in pseudomonas putida. Journal of Bacteriology, 182:6339-6346, Nov 2000. URL: https://doi.org/10.1128/jb.182.22.6339-6346.2000, doi:10.1128/jb.182.22.6339-6346.2000. This article has 193 citations and is from a peer-reviewed journal.
(perez‐pantoja2015thedifferentialresponse pages 23-26): Danilo Pérez‐Pantoja, Juhyun Kim, Rafael Silva‐Rocha, and Víctor de Lorenzo. The differential response of the pben promoter of pseudomonas putida mt-2 to benr and xyls prevents metabolic conflicts in m-xylene biodegradation. Environmental microbiology, 17 1:64-75, Apr 2015. URL: https://doi.org/10.1111/1462-2920.12443, doi:10.1111/1462-2920.12443. This article has 31 citations and is from a domain leading peer-reviewed journal.
(perez‐pantoja2015thedifferentialresponse pages 7-9): Danilo Pérez‐Pantoja, Juhyun Kim, Rafael Silva‐Rocha, and Víctor de Lorenzo. The differential response of the pben promoter of pseudomonas putida mt-2 to benr and xyls prevents metabolic conflicts in m-xylene biodegradation. Environmental microbiology, 17 1:64-75, Apr 2015. URL: https://doi.org/10.1111/1462-2920.12443, doi:10.1111/1462-2920.12443. This article has 31 citations and is from a domain leading peer-reviewed journal.
(perez‐pantoja2015thedifferentialresponse media 32f9b80f): Danilo Pérez‐Pantoja, Juhyun Kim, Rafael Silva‐Rocha, and Víctor de Lorenzo. The differential response of the pben promoter of pseudomonas putida mt-2 to benr and xyls prevents metabolic conflicts in m-xylene biodegradation. Environmental microbiology, 17 1:64-75, Apr 2015. URL: https://doi.org/10.1111/1462-2920.12443, doi:10.1111/1462-2920.12443. This article has 31 citations and is from a domain leading peer-reviewed journal.
(perez‐pantoja2015thedifferentialresponse media 92d90004): Danilo Pérez‐Pantoja, Juhyun Kim, Rafael Silva‐Rocha, and Víctor de Lorenzo. The differential response of the pben promoter of pseudomonas putida mt-2 to benr and xyls prevents metabolic conflicts in m-xylene biodegradation. Environmental microbiology, 17 1:64-75, Apr 2015. URL: https://doi.org/10.1111/1462-2920.12443, doi:10.1111/1462-2920.12443. This article has 31 citations and is from a domain leading peer-reviewed journal.
(hanko2023tfbminerauserfriendly pages 6-7): Erik K. R. Hanko, Tariq A. Joosab Noor Mahomed, Ruth A. Stoney, and Rainer Breitling. Tfbminer: a user-friendly command line tool for the rapid mining of transcription factor-based biosensors. ACS Synthetic Biology, 12:1497-1507, Apr 2023. URL: https://doi.org/10.1021/acssynbio.2c00679, doi:10.1021/acssynbio.2c00679. This article has 20 citations and is from a domain leading peer-reviewed journal.
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