Plasmids in the Biodegradation of Chlorinated Aromatic Compounds

Chatterjee, Deb; Kellogg, S. T.; Watkins, D. R.; Chakrabarty, Ananda M.

doi:10.1007/978-1-4684-3983-0_50

Cited by 18 publications

(11 citation statements)

References 8 publications

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“…Indeed, both P. putida(pAC25) and Pseudomonas sp. strain B13 undergo spontaneous mutation to enable utilization of 3,5-dichlorocatechol (5,7,31,32). Genetic analysis of plasmids derived from pAC27 that are able to degrade dichlorocatechols will be required to demonstrate the acquisition of a complete and functional tfdF-like gene.…”

Section: Cgcatcgtccatcggtcctttactgggtcatccagcccggctccgatatcggcggtctcgmentioning

confidence: 99%

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

et al. 1990

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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...

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Section: Cgcatcgtccatcggtcctttactgggtcatccagcccggctccgatatcggcggtctcgmentioning

confidence: 99%

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

et al. 1990

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“…Studies of certain bacterial strains capable of degrading chlorinated aromatic compounds, such as chlorobenzene [75][76][77][78][79][80], chlorobenzoate [35,36,[81][82][83][84][85], and 2,4dichlorophenoxyacetic acid [86][87][88], demonstrated that ortho-cleavage of aromatic compounds may involve an alternative set of enzymes operating under natural conditions. The majority of these strains convert chlorinated aromatic compounds into chlorine-substituted catechols, which undergo subsequent ortho-cleavage by chlorocatechol-1,2-dioxygenase.…”

Section: Genes Of Ortho-cleavage Of the Aromatic Ringmentioning

confidence: 99%

10.1007/s10438-008-2001-3

2000

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Contemporary data on the mechanism of biodegradation of aromatic hydrocarbons and biodegradation genes (genomic organization and pathways of evolution) in diverse groups of microorganisms have been reviewed. Studies of this problem are topical, in view of the need in identification and construction of new strains degrading xenobiotics, particularly those halogenated. For this reason, emphasis is placed on specific features of explored metabolic pathways that can be used for constructing new enzymatic systems not present in nature. Sections on the mechanisms of genomic rearrangements involving biodegradation determinants are presented from the same standpoint. Part of the review is devoted to analyzing methods used for studying the population dynamics of bacterial communities involved in xenobiotic degradation in natural biotopes or industrial waste disposal plants. Particular attention is given to methods of gene systematics.

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“…Consequently, catechol degrading microorganisms are unable to utilize chlorinated catechols. However, it is possible to isolate from nature various Pseudomonas species and Alcaligenes eutrophus which are capable of degrading chlorinated benzoic acids, phenoxyacetic acids, and benzenes such as 3-chlorobenzoic acid (3-Cba; Chatterjee et al 1981), 2,4-dichlorophenoxyacetic acid (2,4-D; Don & Pemberton 1981) and 1,2,4-trichlorobenzene (1,2,4-Tcb; van der Meer et al 1991a). These compounds are metabolized to their corresponding frame with amino acid identity to TcbR and other regulatory proteins, but its exact function has not been delineated.…”

Section: Environmental Modulation Of Microbial Gene Evolutionmentioning

confidence: 99%

The environment, microbes and bioremediation: microbial activities modulated by the environment

Daubaras

Chakrabarty

1992

Biodegradation

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Microorganisms in nature are largely responsible for the biodegradation and removal of toxic and non-toxic chemicals. Many organisms are also known to have specific ecological niches for proliferation and colonization. The nature of the environment dictates to a large extent the biodegradability of synthetic compounds by modulating the evolutionary processes in microorganisms for new degradative genes. Similarly, environmental factors often determine the extent of microbial gene expression by activating or repressing specific gene or sets of genes through a sensory signal transduction process. Understanding how the environment modulates microbial activity is critical for successful bioremediative applications.

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Plasmids in the Biodegradation of Chlorinated Aromatic Compounds

Cited by 18 publications

References 8 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

10.1007/s10438-008-2001-3

The environment, microbes and bioremediation: microbial activities modulated by the environment

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