Intergeneric evolutionary homology revealed by the study of protocatechuate 3,4-dioxygenase from Azotobacter vinelandii

Durham, D R; Stirling, Lynne A.; Ornston, L N

doi:10.1021/bi00542a023

Cited by 72 publications

(46 citation statements)

References 33 publications

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“…Pseudomonas aeruginosa resembles P. putida in many respects and elaborates closely homologous structural genes (Pate1 & ) that appear to be organized and transcribed in a roughly similar fashion (Kemp & Hegeman, 1968). Azotobacter species possess pca structural genes that are homologous to their P. putida counterparts, and P-ketoadipate elicits a similar inducible response in these two biological groups (Durham & Ornston, 1980). Therefore it will be of interest to determine if homologues of pcaR govern gene expression in Azotobacter.…”

Section: Discussionmentioning

confidence: 99%

“…1). The pathway is distributed widely among bacteria, and comparative studies indicate that structural genes for the pathway in biologically distant prokaryotic groups have evolved from a single ancestral set (Durham & Ornston, 1980;Durham et al, 1980;Yeh etal., 1980a, b;Yeh &Omston, 1981). The divergent genes have fallen under different forms of transcriptional control Stanier & Ornston, 1973;Ornston & Parke, 1977;Cain, 1980;Parke & Ornston, 1986) and thus gene rearrangement appears to have played a significant role in the evolution of the pathway.…”

Section: Introductionmentioning

confidence: 99%

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Cloning and Expression of pca Genes from Pseudomonas putida in Escherichia coli

Mk²,

Je³

et al. 1988

Microbiology

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P-Ketoadipate elicits expression of five structural pca genes encoding enzymes that catalyse consecutive reactions in the utilization of protocatechuate by Pseudomonas putida. Three derivatives of P. putida PRS2000 were obtained, each carrying a single copy of Tn5 DNA inserted into a separate region of the genome and preventing expression of different sets ofpca genes. Selection of Tn5 in or near the pca genes in these derivatives was used to clone four structuralpca genes and to enable their expression as inserts in pUC19 carried in Escherichia coli. Three of the genes were clustered as components of an apparent operon in the order pcaBDC. This observation indicates that rearrangement of the closely linked genes accompanied divergence of their evolutionary homologues, which are known to appear in the orderpcaDBC in the Acinetobacter calcoaceticus pcaEFDBCA gene cluster. Additional evidence for genetic reorganization during evolutionary divergence emerged from the demonstration that the P. putida pcaE gene lies more than 15 kilobase pairs (kbp) away from the pcaBDC operon. An additional P. putida gene, pcaR, was shown to be required for expression of the pca structural genes in response to P-ketoadipate. The regulatory pcaR gene is located about 15 kbp upstream from the pcaBDC operon.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cloning and Expression of pca Genes from Pseudomonas putida in Escherichia coli

Mk²,

Je³

et al. 1988

Microbiology

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“…Both these enzymes are well characterized and found to be heterodimers with α and β subunits and requires Fe +2 for their activity [32,64,67,76,104,109,111,112]. Some of them are reported to be octamers or decamers [5,25,105,108]. In Pseudomonas aeruginosa, protocatechuate 3,4-dioxygenase is a octamer, each subunit of octamer has two α and two β subunits with molecular weight of 22.5 and 25 kD, respectively.…”

Section: Protocatechaute Dioxygenasementioning

confidence: 99%

Bacterial degradation of phthalate isomers and their esters

Vamsee-Krishna

Phale

2008

Indian J Microbiol

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Phthalate isomers and their esters are used heavily in various industries. Excess use and leaching from the product pose them as major pollutants. These chemicals are toxic, teratogenic, mutagenic and carcinogenic in nature. Various aspects like toxicity, diversity in the aerobic bacterial degradation, enzymes and genetic organization of the metabolic pathways from various bacterial strains are reviewed here. Degradation of these esters proceeds by the action of esterases to form phthalate isomers, which are converted to dihydroxylated intermediates by specifi c and inducible phthalate isomer dioxygenases. Metabolic pathways of phthalate isomers converge at 3,4-dihydroxybenzoic acid, which undergoes either ortho-or meta-ring cleavage and subsequently metabolized to the central carbon pathway intermediates. The genes involved in the degradation are arranged in operons present either on plasmid or chromosome or both, and induced by specifi c phthalate isomer. Understanding metabolic pathways, diversity and their genetic regulation may help in constructing bacterial strains through genetic engineering approach for effective bioremediation and environmental clean up.

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“…Both intradiol and extradiol ring cleavage dioxygenases operate in degradation pathways that convert aromatic compounds such as tyrosine and 4-hydroxyphenylacetate to tricarboxcylic acid cycle intermediates (3,7,43,44). DNA and amino acid sequence analyses have shown that the intradiol and extradiol dioxygenases are evolutionarily distinct (15,20,23). There now appear to be at least three phylogenetically distinct families of extradiol dioxygenases (2).…”

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confidence: 99%

A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family

et al. 1995

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Almost all bacterial ring cleavage dioxygenases contain iron as the catalytic metal center. We report here the first available sequence for a manganese-dependent 3,4-dihydroxyphenylacetate (3,4-DHPA) 2,3-dioxygenase and its further characterization. This manganese-dependent extradiol dioxygenase from Arthrobacter globiformis CM-2, unlike iron-dependent extradiol dioxygenases, is not inactivated by hydrogen peroxide. Also, ferrous ions, which activate iron extradiol dioxygenases, inhibit 3,4-DHPA 2,3-dioxygenase. The gene encoding 3,4-DHPA 2,3-dioxygenase, mndD, was identified from an A. globiformis CM-2 cosmid library. mndD was subcloned as a 2.0-kb SmaI fragment in pUC18, from which manganese-dependent extradiol dioxygenase activity was expressed at high levels in Escherichia coli. The mndD open reading frame was identified by comparison with the known N-terminal amino acid sequence of purified manganese-dependent 3,4-DHPA 2,3-dioxygenase. Fourteen of 18 amino acids conserved in members of the iron-dependent extradiol dioxygenase family are also conserved in the manganese-dependent 3,4-DHPA 2,3-dioxygenase (MndD). Thus, MndD belongs to the extradiol family of dioxygenases and may share a common ancestry with the iron-dependent extradiol dioxygenases. We propose the revised consensus primary sequence (G,T,N,R)X(H,A)XXXXXXX(L,I,V,M,F)YXX(D,E,T,N,A)PX(G,P)X{2,3}E for this family. (Numbers in brackets indicate a gap of two or three residues at this point in the sequence.) The suggested common ancestry is also supported by sequence obtained from genes flanking mndD, which share significant sequence identity with xylJ and xylG from Pseudomonas putida.

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Intergeneric evolutionary homology revealed by the study of protocatechuate 3,4-dioxygenase from Azotobacter vinelandii

Cited by 72 publications

References 33 publications

Cloning and Expression of pca Genes from Pseudomonas putida in Escherichia coli

Cloning and Expression of pca Genes from Pseudomonas putida in Escherichia coli

Bacterial degradation of phthalate isomers and their esters

A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family

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