scholarly journals Identification of a Conserved Transcriptional Activator-Repressor Module Controlling the Expression of Genes Involved in Tannic Acid Degradation and Gallic Acid Utilization in Aspergillus niger

2021 ◽  
Vol 2 ◽  
Author(s):  
Mark Arentshorst ◽  
Marcos Di Falco ◽  
Marie-Claude Moisan ◽  
Ian D. Reid ◽  
Tessa O. M. Spaapen ◽  
...  
Keyword(s):  
Gallic Acid ◽  
Tannic Acid ◽  
Acid Metabolism ◽  
Constitutive Expression ◽  
Transcriptional Activator ◽  
Quinic Acid ◽  
Gene Clusters ◽  
Ring Cleavage ◽  
Gene Encoding ◽  
Genes Encoding

Tannic acid, a hydrolysable gallotannin present in plant tissues, consists of a central glucose molecule esterified with gallic acid molecules. Some microorganisms, including several Aspergillus species, can metabolize tannic acid by releasing gallic acid residues from tannic acid by secreting tannic acid specific esterases into the medium. The expression of these so-called tannases is induced by tannic acid or gallic acid. In this study, we identified a conserved transcriptional activator-repressor module involved in the regulation of predicted tannases and other genes involved in gallic acid metabolism. The transcriptional activator-repressor module regulating tannic acid utilization resembles the transcriptional activator-repressor modules regulating galacturonic acid and quinic acid utilization. Like these modules, the Zn(II)2Cys6 transcriptional activator (TanR) and the putative repressor (TanX) are located adjacent to each other. Deletion of the transcriptional activator (ΔtanR) results in inability to grow on gallic acid and severely reduces growth on tannic acid. Deletion of the putative repressor gene (ΔtanX) results in the constitutive expression of tannases as well as other genes with mostly unknown function. Known microbial catabolic pathways for gallic acid utilization involve so-called ring cleavage enzymes, and two of these ring cleavage enzymes show increased expression in the ΔtanX mutant. However, deletion of these two genes, and even deletion of all 17 genes encoding potential ring cleavage enzymes, did not result in a gallic acid non-utilizing phenotype. Therefore, in A. niger gallic acid utilization involves a hitherto unknown pathway. Transcriptome analysis of the ΔtanX mutant identified several genes and gene clusters that were significantly induced compared to the parental strain. The involvement of a selection of these genes and gene clusters in gallic acid utilization was examined by constructing gene deletion mutants and testing their ability to grow on gallic acid. Only the deletion of a gene encoding an FAD-dependent monooxygenase (NRRL3_04659) resulted in a strain that was unable to grow on gallic acid. Metabolomic studies showed accumulation of gallic acid in the ΔNRRL3_04659 mutant suggesting that this predicted monooxygenase is involved in the first step of gallic acid metabolism and is likely responsible for oxidation of the aromatic ring.

scholarly journals Genetic and Functional Investigation of Zn 2 Cys 6 Transcription Factors RSE2 and RSE3 in Podospora anserina

2013 ◽  
Vol 13 (1) ◽  
pp. 53-65 ◽  
Author(s):  
Elodie Bovier ◽  
Carole H. Sellem ◽  
Adeline Humbert ◽  
Annie Sainsard-Chanet
Keyword(s):  
Transcription Factors ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Constitutive Expression ◽  
Podospora Anserina ◽  
Loss Of Function ◽  
Gene Encoding ◽  
Content Type ◽  
Zinc Cluster ◽  
Wide Range ◽  
Genes Encoding

ABSTRACT In Podospora anserina , the two zinc cluster proteins RSE2 and RSE3 are essential for the expression of the gene encoding the alternative oxidase ( aox ) when the mitochondrial electron transport chain is impaired. In parallel, they activated the expression of gluconeogenic genes encoding phosphoenolpyruvate carboxykinase ( pck ) and fructose-1,6-biphosphatase ( fbp ). Orthologues of these transcription factors are present in a wide range of filamentous fungi, and no other role than the regulation of these three genes has been evidenced so far. In order to better understand the function and the organization of RSE2 and RSE3, we conducted a saturated genetic screen based on the constitutive expression of the aox gene. We identified 10 independent mutations in 9 positions in rse2 and 11 mutations in 5 positions in rse3 . Deletions were generated at some of these positions and the effects analyzed. This analysis suggests the presence of central regulatory domains and a C-terminal activation domain in both proteins. Microarray analysis revealed 598 genes that were differentially expressed in the strains containing gain- or loss-of-function mutations in rse2 or rse3 . It showed that in addition to aox , fbp , and pck , RSE2 and RSE3 regulate the expression of genes encoding the alternative NADH dehydrogenase, a Zn 2 Cys 6 transcription factor, a flavohemoglobin, and various hydrolases. As a complement to expression data, a metabolome profiling approach revealed that both an rse2 gain-of-function mutation and growth on antimycin result in similar metabolic alterations in amino acids, fatty acids, and α-ketoglutarate pools.

scholarly journals Virulence of the Phytopathogen Pseudomonas syringae pv. Maculicola Is rpoN Dependent

2000 ◽  
Vol 182 (12) ◽  
pp. 3498-3507 ◽  
Author(s):  
Erik L. Hendrickson ◽  
Pablo Guevera ◽  
Alejandro Peñaloza-Vàzquez ◽  
Jing Shao ◽  
Carol Bender ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Constitutive Expression ◽  
Nitrogen Sources ◽  
Dicarboxylic Acids ◽  
Avirulence Gene ◽  
Gene Encoding ◽  
Direct Role ◽  
Mrna Accumulation ◽  
Genes Encoding ◽  
Mutant Phenotypes

ABSTRACT We cloned the rpoN (ntrA andglnF) gene encoding ς54 from the phytopathogen Pseudomonas syringae pv. maculicola strain ES4326. The P. syringae ES4326 rpoN gene complemented Pseudomonas aeruginosa, Escherichia coli, and Klebsiella aerogenes rpoN mutants for a variety of rpoN mutant phenotypes, including the inability to utilize nitrate as sole nitrogen source. DNA sequence analysis of the P. syringae ES4326 rpoN gene revealed that the deduced amino acid sequence was most similar (86% identity; 95% similarity) to the ς54 protein encoded by thePseudomonas putida rpoN gene. A marker exchange protocol was used to construct an ES4326 rpoN insertional mutation,rpoN::Kmr. In contrast to wild-type ES4326, ES4326 rpoN::Kmr was nonmotile and could not utilize nitrate, urea, C4-dicarboxylic acids, several amino acids, or concentrations of ammonia below 2 mM as nitrogen sources.rpoN was essential for production of the phytotoxin coronatine and for expression of the structural genes encoding coronamic acid. In addition, ES4326rpoN::Kmr did not multiply or elicit disease symptoms when infiltrated into Arabidopsis thalianaleaves, did not elicit the accumulation of severalArabidopsis defense-related mRNAs, and did not elicit a hypersensitive response (HR) when infiltrated into tobacco (Nicotiana tabacum) leaves. Furthermore, whereas P. syringae ES4326 carrying the avirulence gene avrRpt2elicited an HR when infiltrated into Arabidopsis ecotype Columbia leaves, ES4326 rpoN::Kmrcarrying avrRpt2 elicited no response. Constitutive expression of ES4326 hrpL in ES4326rpoN::Kmr partially restored defense-related mRNA accumulation, showing a direct role for thehrp cluster in host defense gene induction in a compatible host-pathogen interaction. However, constitutive expression ofhrpL in ES4326 rpoN::Kmrdid not restore coronatine production, showing that coronatine biosynthesis requires factors other than hrpL.

Gal80 proteins of Kluyveromyces lactis and Saccharomyces cerevisiae are highly conserved but contribute differently to glucose repression of the galactose regulon

1993 ◽  
Vol 13 (12) ◽  
pp. 7566-7576
Author(s):  
F T Zenke ◽  
W Zachariae ◽  
A Lunkes ◽  
K D Breunig
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Sites ◽  
Glucose Repression ◽  
Kluyveromyces Lactis ◽  
Constitutive Expression ◽  
Indirect Evidence ◽  
Transcriptional Activator ◽  
Negative Regulator ◽  
Gene Encoding ◽  
Fold Induction

We cloned the GAL80 gene encoding the negative regulator of the transcriptional activator Gal4 (Lac9) from the yeast Kluyveromyces lactis. The deduced amino acid sequence of K. lactis GAL80 revealed a strong structural conservation between K. lactis Gal80 and the homologous Saccharomyces cerevisiae protein, with an overall identity of 60% and two conserved blocks with over 80% identical residues. K. lactis gal80 disruption mutants show constitutive expression of the lactose/galactose metabolic genes, confirming that K. lactis Gal80 functions in essentially in the same way as does S. cerevisiae Gal80, blocking activation by the transcriptional activator Lac9 (K. lactis Gal4) in the absence of an inducing sugar. However, in contrast to S. cerevisiae, in which Gal4-dependent activation is strongly inhibited by glucose even in a gal80 mutant, glucose repressibility is almost completely lost in gal80 mutants of K. lactis. Indirect evidence suggests that this difference in phenotype is due to a higher activator concentration in K. lactis which is able to overcome glucose repression. Expression of the K. lactis GAL80 gene is controlled by Lac9. Two high-affinity binding sites in the GAL80 promoter mediate a 70-fold induction by galactose and hence negative autoregulation by Gal80. Gal80 in turn not only controls Lac9 activity but also has a moderate influence on its rate of synthesis. Thus, a feedback control mechanism exists between the positive and negative regulators. By mutating the Lac9 binding sites of the GAL80 promoter, we could show that induction of GAL80 is required to prevent activation of the lactose/galactose regulon in glycerol or glucose plus galactose, whereas the noninduced level of Gal80 is sufficient to completely block Lac9 function in glucose.

Characterization of LgnR, an IclR family transcriptional regulator involved in the regulation of l-gluconate catabolic genes in Paracoccus sp. 43P

Microbiology ◽  
2014 ◽  
Vol 160 (3) ◽  
pp. 623-634 ◽  
Author(s):  
Tetsu Shimizu ◽  
Akira Nakamura
Keyword(s):  
Constitutive Expression ◽  
Transcriptional Regulator ◽  
Pcr Analysis ◽  
Mobility Shift ◽  
Gene Encoding ◽  
Reverse Transcription Pcr ◽  
Dnase I Footprinting ◽  
Catabolic Genes ◽  
Genes Encoding ◽  
Mobility Shift Assay

Five genes encoding enzymes required for l-gluconate catabolism, together with genes encoding components of putative ABC transporters, are located in a cluster in the genome of Paracoccus sp. 43P. A gene encoding a transcriptional regulator in the IclR family, lgnR, is located in front of the cluster in the opposite direction. Reverse transcription PCR analysis indicated that the cluster was transcribed as an operon, termed the lgn operon. Two promoters, P lgnA and P lgnR , are divergently located in the intergenic region, and transcription from these promoters was induced by addition of l-gluconate or d-idonate, a catabolite of l-gluconate. Deletion of lgnR resulted in constitutive expression of lgnA, lgnH and lgnR, indicating that lgnR encodes a repressor protein for the expression of the lgn operon and lgnR itself. Electrophoretic mobility shift assay and DNase I footprinting analyses revealed that recombinant LgnR binds to both P lgnA and P lgnR , indicating that LgnR represses transcription from these promoters by competing with RNA polymerase for binding to these sequences. d-Idonate was identified as a candidate effector molecule for dissociation of LgnR from these promoters. Phylogenetic analysis revealed that LgnR formed a cluster with putative proteins from other genome sequences, which is distinct from those proteins of known regulatory functions, in the IclR family of transcriptional regulators. Additionally, the phylogeny suggests an evolutionary linkage between the l-gluconate catabolic pathway and d-galactonate catabolic pathways distributed in Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria and Actinobacteria.

scholarly journals A Physical Map of the Syringomycin and Syringopeptin Gene Clusters Localized to an Approximately 145-kb DNA Region of Pseudomonas syringae pv. syringae Strain B301D

2001 ◽  
Vol 14 (12) ◽  
pp. 1426-1435 ◽  
Author(s):  
Brenda K. Scholz-Schroeder ◽  
Jonathan D. Soule ◽  
Shi-En Lu ◽  
Ingeborg Grgurina ◽  
Dennis C. Gross
Keyword(s):  
Gene Cluster ◽  
Pseudomonas Syringae ◽  
Physical Map ◽  
Regulatory Element ◽  
Gene Clusters ◽  
Gene Encoding ◽  
Peptide Synthetases ◽  
Peptide Synthetase ◽  
Genes Encoding ◽  
Size Estimates

Genetic and phenotypic mapping of an approximately 145-kb DraI fragment of Pseudomonas syringae pv. syringae strain B301D determined that the syringomycin (syr) and syringopeptin (syp) gene clusters are localized to this fragment. The syr and syp gene clusters encompass approximately 55 kb and approximately 80 kb, respectively. Both phytotoxins are synthesized by a thiotemplate mechanism of biosynthesis, requiring large multienzymatic proteins called peptide synthetases. Genes encoding peptide synthetases were identified within the syr and syp gene clusters, accounting for 90% of the DraI fragment. In addition, genes encoding regulatory and secretion proteins were localized to the DraI fragment. In particular, the salA gene, encoding a regulatory element responsible for syringomycin production and lesion formation in P. syringae pv. syringae strain B728a, was localized to the syr gene cluster. A putative ATP-binding cassette (ABC) transporter homolog was determined to be physically located in the syp gene cluster, but phenotypically affects production of both phytotoxins. Preliminary size estimates of the syr and syp gene clusters indicate that they represent two of the largest nonribosomal peptide synthetase gene clusters. Together, the syr and syp gene clusters encompass approximately 135 kb of DNA and may represent a genomic island in P. syringae pv. syringae that contributes to virulence in plant hosts.

scholarly journals Genetic Analysis of Dioxin Dioxygenase ofSphingomonas sp. Strain RW1: Catabolic Genes Dispersed on the Genome

1998 ◽  
Vol 180 (15) ◽  
pp. 3954-3966 ◽  
Author(s):  
Jean Armengaud ◽  
Birgitta Happe ◽  
Kenneth N. Timmis
Keyword(s):  
Supply System ◽  
Ring Cleavage ◽  
Gene Encoding ◽  
Genetic Organization ◽  
Catabolic Genes ◽  
Genes Encoding ◽  
Subsequent Step ◽  
Cleavage Enzyme ◽  
Angular Dioxygenation ◽  
Class Iib

ABSTRACT The dioxin dioxygenase of Sphingomonas sp. strain RW1 activates dibenzo-p-dioxin and dibenzofuran for further metabolism by introducing two atoms of oxygen at a pair of vicinal carbon atoms, one of which is involved in one of the bridges between the two aromatic rings, i.e., an angular dioxygenation. ThedxnA1 and dxnA2 cistrons encoding this dioxygenase have been cloned and shown to be located just upstream of a hydrolase gene which specifies an enzyme involved in the subsequent step of the dibenzofuran biodegradative pathway. Genes encoding the electron supply system of the dioxygenase are not clustered with the dioxygenase gene but rather are located on two other distinct and separate genome segments. Moreover, whereas expression ofdxnA1A2 is modulated according to the available carbon source, expression of the dbfB gene encoding the ring cleavage enzyme of the dibenzofuran pathway, which is located in the neighborhood of dxnA1A2 but oriented in the opposite direction, is constitutive. The scattering of genes for the component proteins of dioxin dioxygenase system around the genome ofSphingomonas sp. strain RW1, and the differential expression of dioxin pathway genes, is unusual and contrasts with the typical genetic organization of catabolic pathways where component cistrons tend to be clustered in multicistronic transcriptional units. The sequences of the α and β subunits of the dioxin dioxygenase exhibit only weak similarity to other three component dioxygenases, but some motifs such as the Fe(II) binding site and the [2Fe-2S] cluster ligands are conserved. Dioxin dioxygenase activity in Escherichia coli cells containing the cloned dxnA1A2 gene was achieved only through coexpression of the cognate electron supply system from RW1. Under these conditions, exclusively angular dioxygenation of dibenzofuran and dibenzo-p-dioxin was obtained. The dioxin dioxygenase was not active in E. colicells coexpressing a class IIB electron supply system. In the course of the isolation of the dxnA1 and dxnA2 cistrons, a number of other catabolic genes dispersed over different genome segments were identified, which may indicate greater catabolic potential than was previously suspected. This finding is consistent with the catabolic versatility of members of the genusSphingomonas, which is becoming increasingly evident, and may indicate a less well evolved and regulated but more dynamic genetic organization in this organism than is the case for better-studied pathways in organisms such as Pseudomonas species.

scholarly journals Genome sequences of Arthrobacter spp. that use a modified sulfoglycolytic Embden-Meyerhof-Parnas pathway

2021 ◽  
Author(s):  
Arashdeep Kaur ◽  
Phillip L van der Peet ◽  
Janice Mui ◽  
Marion Herisse ◽  
Sacha J. Pidot ◽  
...  
Keyword(s):  
Bacterial Communities ◽  
Soil Bacteria ◽  
Gene Clusters ◽  
Soil Samples ◽  
Genome Sequences ◽  
Gram Positive ◽  
Gene Encoding ◽  
The Core ◽  
Genes Encoding ◽  
Australian Soil

Background: Sulfoglycolysis pathways enable the breakdown of the sulfosugar sulfoquinovose and environmental recycling of its carbon and sulfur content. Several pathways exist for the breakdown of sulfoquinovose that usually lead to production of C3-sulfonates (sulfolactate and 2,3-dihydroxypropanesulfonate) that are excreted and sustain secondary bacterial communities. The prototypical sulfoglycolytic pathway is a variant of the classical Embden-Meyerhof-Parnas pathway that has been described in gram-negative Escherichia coli and results in production of 2,3-dihydroxypropanesulfonate. Results: We used enrichment cultures to discover new sulfoglycolytic bacteria from Australian soil samples. Two gram-positive Arthrobacter spp. were isolated that produced sulfolactate as the metabolic end-product. Genome sequences identified a modified sulfoglycolytic Embden-Meyerhof-Parnas (sulfo-EMP) gene cluster that retained the core sulfoglycolysis genes encoding metabolic enzymes, but featuring the replacement of the gene encoding sulfolactaldehyde (SLA) reductase with SLA dehydrogenase, and the absence of sulfoquinovosidase and sulfoquinovose mutarotase genes. The gene clusters were broadly conserved across a range of other sequenced Actinobacteria. Conclusions: We report the first gram-positive soil bacteria that utilize sulfo-EMP pathways to metabolize SQ. Excretion of sulfolactate is consistent with an aerobic saprophytic lifestyle. This work broadens our knowledge of the sulfo-EMP pathway to include soil bacteria.

scholarly journals The Transcriptional Activator XlnR Regulates Both Xylanolytic and Endoglucanase Gene Expression inAspergillus niger

1998 ◽  
Vol 64 (10) ◽  
pp. 3615-3619 ◽  
Author(s):  
Noël N. M. E. van Peij ◽  
Marco M. C. Gielkens ◽  
Ronald P. de Vries ◽  
Jaap Visser ◽  
Leo H. de Graaff
Keyword(s):  
Cellulose Degradation ◽  
Mrna Level ◽  
Transcriptional Activator ◽  
Feruloyl Esterase ◽  
Loss Of Function ◽  
Gene Encoding ◽  
Xylan Degradation ◽  
Genes Encoding ◽  
Encoding Genes ◽  
Xylanolytic Enzymes

ABSTRACT The expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungusAspergillus niger. A strain with a loss-of-function mutation in the xlnR gene encoding the transcriptional activator XlnR and a strain with multiple copies of this gene were investigated in order to define which genes are controlled by XlnR. The data presented in this paper show that the transcriptional activator XlnR regulates the transcription of thexlnB, xlnC, and xlnD genes encoding the main xylanolytic enzymes (endoxylanases B and C and β-xylosidase, respectively). Also, the transcription of the genes encoding the accessory enzymes involved in xylan degradation, including α-glucuronidase A, acetylxylan esterase A, arabinoxylan arabinofuranohydrolase A, and feruloyl esterase A, was found to be controlled by XlnR. In addition, XlnR also activates transcription of two endoglucanase-encoding genes, eglA andeglB, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endoglucanase-encoding genes.

scholarly journals Gal80 proteins of Kluyveromyces lactis and Saccharomyces cerevisiae are highly conserved but contribute differently to glucose repression of the galactose regulon.

1993 ◽  
Vol 13 (12) ◽  
pp. 7566-7576 ◽  
Author(s):  
F T Zenke ◽  
W Zachariae ◽  
A Lunkes ◽  
K D Breunig
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Sites ◽  
Glucose Repression ◽  
Kluyveromyces Lactis ◽  
Constitutive Expression ◽  
Indirect Evidence ◽  
Transcriptional Activator ◽  
Negative Regulator ◽  
Gene Encoding ◽  
Fold Induction

We cloned the GAL80 gene encoding the negative regulator of the transcriptional activator Gal4 (Lac9) from the yeast Kluyveromyces lactis. The deduced amino acid sequence of K. lactis GAL80 revealed a strong structural conservation between K. lactis Gal80 and the homologous Saccharomyces cerevisiae protein, with an overall identity of 60% and two conserved blocks with over 80% identical residues. K. lactis gal80 disruption mutants show constitutive expression of the lactose/galactose metabolic genes, confirming that K. lactis Gal80 functions in essentially in the same way as does S. cerevisiae Gal80, blocking activation by the transcriptional activator Lac9 (K. lactis Gal4) in the absence of an inducing sugar. However, in contrast to S. cerevisiae, in which Gal4-dependent activation is strongly inhibited by glucose even in a gal80 mutant, glucose repressibility is almost completely lost in gal80 mutants of K. lactis. Indirect evidence suggests that this difference in phenotype is due to a higher activator concentration in K. lactis which is able to overcome glucose repression. Expression of the K. lactis GAL80 gene is controlled by Lac9. Two high-affinity binding sites in the GAL80 promoter mediate a 70-fold induction by galactose and hence negative autoregulation by Gal80. Gal80 in turn not only controls Lac9 activity but also has a moderate influence on its rate of synthesis. Thus, a feedback control mechanism exists between the positive and negative regulators. By mutating the Lac9 binding sites of the GAL80 promoter, we could show that induction of GAL80 is required to prevent activation of the lactose/galactose regulon in glycerol or glucose plus galactose, whereas the noninduced level of Gal80 is sufficient to completely block Lac9 function in glucose.

scholarly journals Cloning and Characterization of lin Genes Responsible for the Degradation of Hexachlorocyclohexane Isomers by Sphingomonas paucimobilis Strain B90

2002 ◽  
Vol 68 (12) ◽  
pp. 6021-6028 ◽  
Author(s):  
Rekha Kumari ◽  
Sanjukta Subudhi ◽  
Mrutyunjay Suar ◽  
Gauri Dhingra ◽  
Vishakha Raina ◽  
...  
Keyword(s):  
Ring Cleavage ◽  
Sphingomonas Paucimobilis ◽  
Agricultural Pests ◽  
Gene Encoding ◽  
Public Health Programs ◽  
Hch Isomers ◽  
Gene Coding ◽  
Genes Encoding ◽  
Gene Structures

ABSTRACT Hexachlorocyclohexane (HCH) has been used extensively against agricultural pests and in public health programs for the control of mosquitoes. Commercial formulations of HCH consist of a mixture of four isomers, α, β, γ, and δ. While all these isomers pose serious environmental problems, β-HCH is more problematic due to its longer persistence in the environment. We have studied the degradation of HCH isomers by Sphingomonas paucimobilis strain B90 and characterized the lin genes encoding enzymes from strain B90 responsible for the degradation of HCH isomers. Two nonidentical copies of the linA gene encoding HCH dehydrochlorinase, which were designated linA1 and linA2, were found in S. paucimobilis B90. The linA1 and linA2 genes could be expressed in Escherichia coli, leading to dehydrochlorination of α-, γ-, and δ-HCH but not of β-HCH, suggesting that S. paucimobilis B90 contains another pathway for the initial steps of β-HCH degradation. The cloning and characterization of the halidohydrolase (linB), dehydrogenase (linC and linX), and reductive dechlorinase (linD) genes from S. paucimobilis B90 revealed that they share ∼96 to 99% identical nucleotides with the corresponding genes of S. paucimobilis UT26. No evidence was found for the presence of a linE-like gene, coding for a ring cleavage dioxygenase, in strain B90. The gene structures around the linA1 and linA2 genes of strain B90, compared to those in strain UT26, are suggestive of a recombination between linA1 and linA2, which formed linA of strain UT26.

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