Partial nucleotide sequence of the chlorocatechol degradative operontfdCDEFof pJP4 and similarity to promoters of the chlorinated aromatic degradative operonstfdAandclcABD

Perkins, Edward J.; Bolton, George; Gordon, Milton P.; Lurquin, Paul F.

doi:10.1093/nar/16.14.7200

Cited by 20 publications

(20 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Genes tfdB and tfdCDEF have been mapped to a 6-kb region of EcoRI fragment B of pJP4 (11). The sequences of the 1.5-kb HindIII G fragment containing tfdC and a portion of tfdD have been determined by Ghosal and You (15) and Perkins et al (29). To complete the sequence of the tfdB and tfdCDEF operons, a 6.2-kb HindIII-SstI fragment of pEP102 was sequenced and joined to that of the 1.5-kb HindIII fragment by sequencing of a 312-base-pair (bp) HindIII fragment from pRD25A.…”

Section: Resultsmentioning

confidence: 99%

“…In addition to a conserved operon structure (Fig. 7) The promoters of tfdBCDEF and clcABD, in addition to tfdA, have a region between -33 and -86 relative to the transcriptional start of clcABD resembling a conserved operator region (29). Interestingly, in pAC27, this region of identity abuts a proposed Pseudomonas aeruginosa and E. coli u70-binding site (9).…”

Section: Cgcatcgtccatcggtcctttactgggtcatccagcccggctccgatatcggcggtctcgmentioning

confidence: 99%

See 1 more Smart Citation

Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

et al. 1990

View full text Add to dashboard Cite

Growth of Alcaligenes eutrophus JMP134 on 2,4-dichlorophenoxyacetate requires a 2,4-dichlorophenol hydroxylase encoded by gene tfdB. Catabolism of either 2,4-dichlorophenoxyacetate or 3-chlorobenzoate involves enzymes encoded by the chlorocatechol oxidative operon consisting of tfdCDEF, which converts 3-chloro-and 3,5-dichlorocatechol to maleylacetate and chloromaleylacetate, respectively. Transposon mutagenesis has localized tfdB and t.fdCDEF to EcoRI fragment B of plasmid pJP4 (R. H. Don, A. J. Wieghtman, H.-J. Knackmuss, and K. N. Timmis, J. Bacteriol. 161:85-90, 1985). We present the complete nucleotide sequence of tfdB and tfdCDEF contained within a 7,954-base-pair HindIII-SstI fragment from EcoRI fragment B. Sequence and expression analysis of tfdB in Escherichia coli suggested that 2,4-dichlorophenol hydroxylase consists of a single subunit of 65 kilodaltons. The amino acid sequences of proteins encoded by tfdD and tfdE were found to be 63 and 53% identical to those of functionally similar enzymes encoded by clcB and ckD, respectively, from plasmid pAC27 of Pseudomonas putida. P. putida(pAC27) can utilize 3-chlorocatechol but not dichlorinated catechols. A region of DNA adjacent to clcD in pAC27 was found to be 47% identical in amino acid sequence to tfdiF, a gene important in catabolizing dichlorocatechols. The region in pAC27 does not appear to encode a protein, suggesting that the absence of a functional trans-chlorodienelactone isomerase may prevent P. putida(pAC27) from utilizing 3,5-dichlorocatechol.Bacteria play a crucial role in the dissimilation of environmental pollutants. In general, the catabolism of aromatic compounds is channeled through catechol intermediates (33). Hence, the ability of an organism to form and catabolize catechols or their derivatives can play a major part in the utilization of an aromatic compound. Comparison of the degradative pathways of different aromatics may help in understanding the evolution of growth substrate specificity.Chlorinated aromatics, such as 2,4-dichlorophenoxyacetic acid (2,4D) and 3-chlorobenzoate (3CBA), are catabolized via a modified ortho pathway (11,12,20,28,34,35; for a review, see reference 33). Pseudomonas putida plasmid pAC27, a deletion derivative of pAC25, confers catabolism of 3CBA (5), whereas Alcaligenes eutrophus JMP134 plasmid pJP4 enables degradation of both 2,4D and 3CBA (10, 11). In both cases, 3CBA appears to be degraded to 3-chlorocatechol by enzymes encoded by chromosomal genes. 2,4D is catabolized by A. eutrophus JMP134 to 2,4-dichlorophenol (2,4DCP) by 2,4D monooxygenase. 2,4DCP is then hydroxylated by 2,4DCP hydroxylase to form 3,5-dichlorocatechol (11; Fig. 1).3-Chlorocatechol is oxidized to maleylacetic acid by enzymes encoded by the clcABD operon in pAC27 (13) and by the tfdCDEF operon of pJP4 (11). The maleylacetic acid is then catabolized by chromosomally encoded enzymes (21). Enzymes involved in this transformation are chlorocatechol 1,2-dioxygenase (catechol 1,2-dioxygenase II or pyrocatechase II; EC 1.13.11.1), encoded b...

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Cgcatcgtccatcggtcctttactgggtcatccagcccggctccgatatcggcggtctcgmentioning

confidence: 99%

Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

et al. 1990

View full text Add to dashboard Cite

show abstract

“…Most of these proteins are involved in amino acid biosynthesis, but two of them (NodD and TfdO) are involved in recognizing or metabolizing phenolic compounds (14,38,47). Most of them activate transcription of genes or operons which are transcribed divergently from their own promoter regions (24), in a situation analogous to the positions of ChvE and ORF1.…”

Section: Resultsmentioning

confidence: 99%

A chromosomal Agrobacterium tumefaciens gene required for effective plant signal transduction

et al. 1990

View full text Add to dashboard Cite

The vir gene products of Agrobactenium tumefaciens carry out the transfer of T-DNA to the plant genome. Effective transcriptional induction of the vir genes by plant signal molecules is controlled by two vir gene products, VirA and VirG. In this study we have identified and cloned a chromosomal region which is also required for vir gene induction. Transposon insertions within this region reduce induction significantly and strongly attenuate virulence, resulting in a restricted host range for infection. The reduction in vir gene transcription can be partially overcome by high concentrations of the inducer molecule acetosyringone. Expression of virG at low pH and low phosphate concentrations, which is independent of plant signals, is not affected by these mutations. Sequence analysis of the region revealed two divergent open reading frames, which we have designated chvE and ORF1. Several transposon insertions mapped in chvE; this resulted in attenuated virulence. chvE codes for a putative protein which is homologous to two periplasmic receptor proteins involved in chemotaxis and uptake of sugars. Whether ORF1 is required for virulence is uncertain. One transposon insertion resulting in avirulence maps in or near the 5' end of ORF1, and several which do not affect virulence map in its 3' end. ORF1 codes for a putative protein which is homologous to a family of transcriptional activator proteins.Strains of Agrobacterium tumefaciens containing a Ti plasmid can incite crown gall tumors on most dicotyledonous and some monocotyledonous plants. Two regions of the Ti plasmid, the transferred DNA (T-DNA) and virulence (vir) regions, are necessary for tumor formation. During infection of wounded plant tissue, the T-DNA is transferred and integrated into the plant nuclear DNA (6,49), where its expression results in crown gall tumor formation (12,18,53). In addition to the Ti plasmid virulence genes, chromosomal genes chvA, chvB, and exoC are required for complete virulence (3, 11). The functioning of these genes is required for attachment of the bacteria to plant cells.Transcription of the vir genes is induced by phenolic compounds, such as acetosyringone, synthesized by wounded plant cells (43,44). The induction system is controlled by two of the vir genes, virA and virG (45, 54 The host range for Agrobacterium infection is determined largely by the T-DNA and vir regions of the Ti plasmid (28,29,35,50). Increasing the expression of certain vir genes increases the virulence and host range of the bacteria (25). However, several observations have indicated that chromosomal genes are also involved in determining host range (17,20). In this study, we found that chromosomal host range mutants originally isolated by Garfinkel and Nester (17) are defective in vir gene induction. MATERIALS AND METHODSBacterial strains, plasmids, and media. Escherichia coli DH5(x, HB101 (1), and SF800 (22)

show abstract

“…There is evidence that TfdR and TfdS are encoded by identical open reading frames and are the result of a gene duplication (55). However, other reports suggest differing repressing and/or activating functions and differing sites of actions for TfdR and TfdS (23,27,28 (40) indicate that the tfdCDEF promoter region bears strong similarity to the known binding site for CatR at the catBC promoter and to the promoter region of clcABD (39), suggesting that a LysR family member, possibly TfdS, does regulate tfdCDEF.…”

Section: Discussionmentioning

confidence: 99%

“…Cells not pregrown on 3Cba were not induced by 3Cba during the 2-h time course of the experiment (13). More recently, a computer homology search (39) of the previously published clcABD operon revealed a partial open reading frame upstream of clcA that was similar to the N terminus of LysR family regulatory proteins (24). The predicted gene would be transcribed divergently from the clcABD operon.…”

mentioning

confidence: 99%

Nucleotide sequence and initial functional characterization of the clcR gene encoding a LysR family activator of the clcABD chlorocatechol operon in Pseudomonas putida

et al. 1993

View full text Add to dashboard Cite

The 3-chlorocatechol operon ckcABD is central to the biodegradative pathway of 3-chlorobenzoate. The ckcR regulatory gene, which activates the ckABD operon, was cloned from the region immediately upstream of the operon and was shown to complement an insertion mutation for growth on 3-chlorobenzoate. ClcR activated the ckcA promoter, which controls expression of the clABD operon, in trans by 14-fold in an in vivo promoter probe assay in Pseudomonas putida when cells were incubated with 15 mM 3-chlorobenzoic acid. Specific binding of ClcR to the clcR-ckA intergenic promoter region was observed in a gel shift assay. Nucleotide sequence analysis of the ckcR gene predicts a polypeptide of 32.5 kDa, which was confirmed by using specific in vivo 35s labeling of the protein from a T7 promoter-controlled ATG fusion construct. ClcR shares high sequence identity with the LysR family of bacterial regulator proteins and has especially high homology to a subgroup of the family consisting of TcbR (57% amino acid sequence identity), TfdS, CatR, and CatM. ClcR was shown to autoregulate its own production in trans to 35% of unrepressed levels but partially relieved this autorepression under conditions that induced transcription at the ckcA promoter. Several considerations indicate that the ckcR-ckABD locus is most similar to the tcbR-tcbCDEF regulon.Modified ortho cleavage pathways are responsible for the biodegradation of a large array of chloroaromatic compounds and are widespread in soil bacterial communities. A well-characterized group of modified ortho cleavage pathway operons that encode functions for the dissimilation of catechol and chlorocatechols provides a model system for studying the regulation of evolutionarily related pathways. These include operons in degradative pathways for 3-chlorobenzoic acid (3Cba) from Pseudomonas putida, 1,2,4-trichlorobenzene from a Pseudomonas sp., 2,4-dichlorophenoxyacetic acid from Alcaligenes eutrophus, and benzoic acid from P. putida and from Acinetobacter calcoaceticus. In the above order, the relevant operons of the first three pathways include clcABD (15), tcbCDEF (50), and tfdCDEF (12), which convert 3-chlorocatechol, 3,4,6-trichlorocatechol, and 3,5-dichlorocatechol to maleylacetic acid, 5-chloromaleylacetic acid, and 2-chloromaleylacetic acid, respectively (12,14,44,45,52). The catechol-degradative genes in the benzoate pathways of P. putida andA. calcoaceticus are clustered in dissimilar operons. In P. putida (after the conversion of catechol to cis,cis-muconate by the catA gene product), the catBC operon encodes the conversion of the latter to 13-ketoadipate enol lactone, which is then transformed to 0-ketoadipate through the action of other loci (36).Catechol degradation in A. calcoaceticus is directed by the catA gene and the catBCEFD operon, which convert catechol through 13-ketoadipate to succinyl coenzyme A and acetyl coenzyme A (36). In nearly every case, the analogous reactions of the above five operons are catalyzed by homologous enzymes.Transcription of the catBCEFD, ...

show abstract

Partial nucleotide sequence of the chlorocatechol degradative operontfdCDEFof pJP4 and similarity to promoters of the chlorinated aromatic degradative operonstfdAandclcABD

Cited by 20 publications

References 6 publications

Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4

A chromosomal Agrobacterium tumefaciens gene required for effective plant signal transduction

Nucleotide sequence and initial functional characterization of the clcR gene encoding a LysR family activator of the clcABD chlorocatechol operon in Pseudomonas putida

Contact Info

Product

Resources

About