Growth of an estuarinePseudomonas sp. on polychlorinated biphenyl

Sayler, Gary S.; Shon, Myung-Baek; Colwell, Rita R.

doi:10.1007/bf02010621

Cited by 40 publications

(17 citation statements)

References 22 publications

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“…All biphenyl dioxygenases isolated from Gram-positive rhodococcal (Actinobacteria) known to date cluster in a single branch whereas BphAs from Proteobacteria are distributed into two distinct families. Among our test strains, strain LB400 and H850 BphA belong to one of these families along with Pseudomonas pseudoalcaligenes KF707 BphA1 [Taira et al, 1992] [Parsons et al, 1988], Pseudomonas sp strain KKS102 [Fukuda et al, 1994], Comamonas testosteroni TK102 [Hiraoka et al, 2002] and from the Cupriavidus necator strain A5 (transposon Tn4371) [Merlin et al, 1997;Sayler et al, 1977] which are also well characterized BphAs. Phylogenetic trees drawn on the basis of the ClustalW sequence alignment of the portion of bphA from bp 480 to bp 1350 of LB400 bphA or of the deduced amino acid fragment corresponding to BphA Cterminal domain are similar to trees drawn based on alignment of whole gene ( fig.…”

Section: Family Clustering Of Bphas From Cultured Bacteriamentioning

confidence: 99%

Diversity of the C-Terminal Portion of the Biphenyl Dioxygenase Large Subunit

Vézina¹,

Barriault²,

Sylvestre³

2008

Microb Physiol

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The biphenyl dioxygenase (BPDO) catalyses a stereospecific dioxygenation of biphenyl and analogs of it. Aside from being involved in the destruction and detoxification of toxic pollutants in soil, in the context of the green chemistry concept, this enzyme is a promising biocatalyst to design new more selective and more environmentally friendly approaches to manufacture fine chemicals. At this time, most of our knowledge about the variability of key residues determining the substrate specificity and regiospecificity of the enzyme oxygenase component (BphAE) toward biphenyl analogs and about the effect of altering these residues on catalytic properties is based on investigations made with BphAEs from cultured organisms and engineered enzymes derived from them. The purpose of this work was to examine the diversity of the amino acid sequence patterns of the α subunit (BphA) C-terminal domain deduced from PCR products amplified from DNA extracted from cultured bacteria of various phylogenetic lines and from the soil microflora of PCB-contaminated soils. Of special interest were segments of the C-terminal portion called regions I, III and IV. Altogether, the phylogenetic tree obtained from aligning the deduced amino acid sequences of BphAs C-terminal domain from cultured bacteria belonging to various ecological niches and from uncultured soil bacteria reveals that most of the BphAs were linked to the three clusters of BphAs previously reported. However, few belong to new branches that diverge from the previously known branches showing a high diversity of BphAs in natural environment. Furthermore, data show a wide distribution of BphAs with family linkages that not only crosses bacterial taxonomic frontiers but also ecological niches. Nevertheless, in spite of this divergence, the sequence patterns of regions III and IV amino acids that are known to influence substrate specificity and regiospecificity are rather conserved among BphAs and the pattern was independent of the family cluster to which they belong. In most cases, regions III and IV amino acid patterns are closer to those of Pseudomonas pseudoalcaligenes KF707 BphA1 than to the most versatile Burkholderia xenovorans LB400 BphA. This might suggest that the PCB-degrading potency of soil bacteria is closer to the one observed for KF707 BphAE than from LB400 BphAE. However, the fact that among less than 20 PCR products amplified from soil DNA that we have sequenced, one of them was very homologous to that of LB400 BphA and in addition, residues 335 and 336 of LB400 were replaced by residues that previous enzyme engineering had shown to extend the range of PCB substrate used by the enzyme strongly suggest that PCB-degrading bacteria are evolving in soil to optimize their PCB-degrading capacity.

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Section: Family Clustering Of Bphas From Cultured Bacteriamentioning

confidence: 99%

Diversity of the C-Terminal Portion of the Biphenyl Dioxygenase Large Subunit

Vézina¹,

Barriault²,

Sylvestre³

2008

Microb Physiol

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“…At concentrations between 100/ig/l and 10mg/l most of the radiolabel ended up in the biomass. 31 Once again the less chlorinated components of the mixture were degraded most readily. The extent of degradation of this mixture in samples of reservoir water depends on the time of year the sample is taken and on the site of sampling.…”

Section: Metabolism Of Pcb Mixturesmentioning

confidence: 99%

Microbial metabolism of chlorobiphenyls

Parsons¹,

Veerkamp²,

Hutzinger³

1983

Toxicological & Environmental Chemistry

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“…Bacteria able to degrade PCBs aerobically are from the genera Pseudomonas, Alcaligenes, Arthrobacter and Acinetobacter. In all PCB-degrading strains the major pathway by which PCBs are biodegraded involves initial dioxygenation to form metabolites hydroxylated in the 2 and 3 positions which are degraded in turn by meta ring cleavage to ultimately give chlorinated benzoic acids (11)(12)(13)(14)(15)(16)(17). In previous reports Alcaligenes strains were capable of cometabolizing a variety of PCB compounds (13,14,(17)(18)(19).…”

Section: Introductionmentioning

confidence: 99%

Biodegradability of tetrachlorobenzyltoluenes and polychlorinated biphenyls in activated sludge and in cultures of alcaligenes sp. JB1: A preliminary study

et al. 1995

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UvA-DARE is a service provided by the library of the University of Amsterdam (http://dare.uva.nl) UvA-DARE (Digital Academic Repository)Biodegradability of tetrachlorobenzyltoluenes and polychlorinated biphenyls in activated sludge and in cultures of Alcaligenes sp. JB1: a preliminary study. van Haelst, A.G.; Bakboord, J.; Parsons, J.R.; Govers, H.A.J. Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 09 May 2018Pergamon 0045-6535(95)00144-1Chemosphere, Vol. 31, No. 3, pp. 2799-2808, 1995 Copyright © 1995 Elsevier Science Ltd Printed in Great Britain. All rights reserved 0045-6535/95 $9.50+0.00 BIODEGRADABILITY OF TETRACHLOROBENZYLTOLUENES ABSTRACTThe biodegradability of tetrachlorobenzyltoluenes (TCBTs) and polychlorinated biphenyls (PCBs) was investigated in activated sludge and in batch cultures of the PCB-degrading microorganism Alcaligenes sp.JB1. There was no evidence for significant biodegradation of either TCBTs or PCBs in activated sludge. In contrast, cultures of strain JB1 did degrade PCB 40, but again there was no evidence for degradation of TCBTs. Although no final conclusions can be drawn from these results about the biodegradability of TCBTs, they do indicate that TCBTs are environmentally persistent compounds.

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Growth of an estuarinePseudomonas sp. on polychlorinated biphenyl

Cited by 40 publications

References 22 publications

Diversity of the C-Terminal Portion of the Biphenyl Dioxygenase Large Subunit

Diversity of the C-Terminal Portion of the Biphenyl Dioxygenase Large Subunit

Microbial metabolism of chlorobiphenyls

Biodegradability of tetrachlorobenzyltoluenes and polychlorinated biphenyls in activated sludge and in cultures of alcaligenes sp. JB1: A preliminary study

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