Evidence map›Paper›PMID 16517628›Full record

ArticleApplied and environmental microbiology2006

Characterization of the terephthalate degradation genes of Comamonas sp. strain E6.

Mikio Sasoh, Eiji Masai, Satoko Ishibashi, Hirofumi Hara, Naofumi Kamimura, Keisuke Miyauchi, Masao Fukuda

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
2.4field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

61 citing papers in PubMed, 146 citations in OpenAlex.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Mikio SasohDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan.
Eiji Masai
Satoko Ishibashi
Hirofumi Hara
Naofumi Kamimura
Keisuke Miyauchi
Masao Fukuda
Nagaoka University of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We isolated Comamonas sp. strain E6, which utilizes terephthalate (TPA) as the sole carbon and energy source via the protocatechuate (PCA) 4,5-cleavage pathway. Two almost identical TPA degradation gene clusters, tphRICIA2IA3IBIA1I and tphRIICIIA2IIA3IIBIIA1II, were isolated from this strain. Based on amino acid sequence similarity, the genes tphR, tphC, tphA2, tphA3, tphB, and tphA1 were predicted to code, respectively, for an IclR-type transcriptional regulator, a periplasmic TPA binding receptor, the large subunit of the oxygenase component of TPA 1,2-dioxygenase (TPADO), the small subunit of the oxygenase component of TPADO, a 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate (DCD) dehydrogenase, and a reductase component of TPADO. The growth of E6 on TPA was not affected by disruption of either tphA2I or tphA2II singly; however, the tphA2I tphA2II double mutant no longer grew on TPA, suggesting that both TPADO genes are involved in TPA degradation. Introduction of a plasmid carrying tphRIICIIA2IIA3IIBIIA1II conferred the TPA utilization phenotype on Comamonas testosteroni IAM 1152, which is able to grow on PCA but not on TPA. Disruption of either tphRII or tphCII on this plasmid resulted in the loss of the growth of IAM 1152 on TPA, suggesting that these genes are essential to convert TPA to PCA in E6. The genes tphA1II, tphA2II, tphA3II, and tphBII were expressed in Escherichia coli, and the resultant cell extracts containing TphA1II, TphA2II, and TphA3II converted TPA in the presence of NADPH into a product which was transformed to PCA by TphBII. On the basis of these results, TPADO was strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase (TphA1), and tphB codes for the DCD dehydrogenase.

Indexed as

Bacterial ProteinsBiodegradation, EnvironmentalComamonasComamonas testosteroniDioxygenasesHydroxybenzoatesMolecular Sequence DataMultigene FamilyMutationOxidation-ReductionPhthalic AcidsSequence Analysis, DNABacterial ProteinsDioxygenasesHydroxybenzoatesPhthalic Acidsprotocatechuic acidterephthalic acid

Identifiers

PMID16517628
PMCPMC1393238
OpenAlexW4248885898

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.