Purification of the LysR family regulator, ClcR, and its interaction with the Pseudomonas putida clcABD chlorocatechol operon promoter

Coco, Wayne M.; Parsek, Matthew R.; Chakrabarty, Ananda M.

doi:10.1128/jb.176.17.5530-5533.1994

Cited by 33 publications

(29 citation statements)

References 15 publications

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“…Strangely, XylS-mediated transcription activation from the P m promoter is independent of 70 -RNAP (136) but during exponential growth is dependent on the alternative sigma factor 32 , which normally is involved in the heat shock response (135). This has led to the suggestion that the presence of the chemical effector m-toluate is triggering a similar response for the cell to the heat shock response.…”

Section: Mechanisms Of Activationmentioning

confidence: 99%

“…The different interactions are explained in more detail for ClcR. ClcR binds the clcA promoter irrespective of the presence of inducer (32,141,182). However, in the absence of inducer, ClcR protects a 27-bp region (RBS) from Ϫ79 to Ϫ53 and a 10-bp region (activator binding site [ABS]) from Ϫ37 to Ϫ28 relative to the transcription start site.…”

Section: Mechanisms Of Activationmentioning

confidence: 99%

“…All the evidence presented so far points to tetramers being the active form of LTTRs. ClcR and CatR have been identified as dimers in solution (32,181), but two dimers are needed to bind DNA (141). CatM, BenM, and CbnR were found to form tetramers (20,30,155), and NahR probably also acts as a tetrameric form (226).…”

Section: Structure and Conformationmentioning

confidence: 99%

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Bacterial Transcriptional Regulators for Degradation Pathways of Aromatic Compounds

Tropel

Meer

2004

Microbiol Mol Biol Rev

340

338

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Human activities have resulted in the release and introduction into the environment of a plethora of aromatic chemicals. The interest in discovering how bacteria are dealing with hazardous environmental pollutants has driven a large research community and has resulted in important biochemical, genetic, and physiological knowledge about the degradation capacities of microorganisms and their application in bioremediation, green chemistry, or production of pharmacy synthons. In addition, regulation of catabolic pathway expression has attracted the interest of numerous different groups, and several catabolic pathway regulators have been exemplary for understanding transcription control mechanisms. More recently, information about regulatory systems has been used to construct whole-cell living bioreporters that are used to measure the quality of the aqueous, soil, and air environment. The topic of biodegradation is relatively coherent, and this review presents a coherent overview of the regulatory systems involved in the transcriptional control of catabolic pathways. This review summarizes the different regulatory systems involved in biodegradation pathways of aromatic compounds linking them to other known protein families. Specific attention has been paid to describing the genetic organization of the regulatory genes, promoters, and target operon(s) and to discussing present knowledge about signaling molecules, DNA binding properties, and operator characteristics, and evidence from regulatory mutants. For each regulator family, this information is combined with recently obtained protein structural information to arrive at a possible mechanism of transcription activation. This demonstrates the diversity of control mechanisms existing in catabolic pathways

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Section: Mechanisms Of Activationmentioning

confidence: 99%

Section: Mechanisms Of Activationmentioning

confidence: 99%

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Bacterial Transcriptional Regulators for Degradation Pathways of Aromatic Compounds

Tropel

Meer

2004

Microbiol Mol Biol Rev

340

338

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“…5B, lane 2). Three sites in this region resemble a consensus binding sequence for LysR-type regulators of the subclass to which BenM and CatM belong (29). These sites are marked in Figs.…”

Section: Benm Is Tetramericmentioning

confidence: 99%

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

Bundy

Collier

Hoover

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

129

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BenM is a LysR-type bacterial transcriptional regulator that controls aromatic compound degradation in Acinetobacter sp. ADP1. Here, in vitro transcription assays demonstrated that two metabolites of aromatic compound catabolism, benzoate and cis,cismuconate, act synergistically to activate gene expression. The level of BenM-regulated benA transcription was significantly higher in response to both compounds than the combined levels due to each alone. These compounds also were more effective together than they were individually in altering the DNase I footprint patterns of BenM-DNA complexes. This type of dual-inducer synergy provides great potential for rapid and large modulations of gene expression and may represent an important, and possibly widespread, feature of transcriptional control.

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“…The TcbR and ClcR regulatory proteins have already been studied in great detail. The binding of the proteins to their target promoter DNA has been reported and described meticulously (4,25). Binding of the TfdR protein to the tfdD II promoter region has also been demonstrated (27), but regulation of this gene by TfdR has not yet been established.…”

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confidence: 99%

The tfdR gene product can successfully take over the role of the insertion element-inactivated TfdT protein as a transcriptional activator of the tfdCDEF gene cluster, which encodes chlorocatechol degradation in Ralstonia eutropha JMP134(pJP4)

Leveau

Meer

1996

J Bacteriol

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The tfdT gene is located upstream of and transcribed divergently from the tfdCDEF chlorocatechol-degradative operon on plasmid pJP4 of Ralstonia eutropha (formerly Alcaligenes eutrophus) JMP134. It is 684 bp long and encodes a 25-kDa protein. On the basis of its predicted amino acid sequence, the TfdT protein could be classified as a LysR-type transcriptional regulator. It has the highest degree of similarity with the proteins TcbR, ClcR, and TfdR, which are involved in the regulation of chloroaromatic breakdown. Despite this homology, the TfdT protein failed to activate the expression of its presumed target operon, tfdCDEF. This failure could be attributed to the inability of TfdT to bind the tfdC promoter region, an absolute requirement for transcriptional activation. Sequence analysis downstream of the tfdT gene revealed the presence of an insertion element-like element. We postulate that this element disrupted the tfdT open reading frame, leading to a premature termination and the production of a truncated, disfunctional TfdT protein. As an alternative to the inactivated TfdT protein, we propose that the product of the tfdR gene (or its identical twin, tfdS), located elsewhere on plasmid pJP4, can successfully take over the regulation of tfdCDEF expression. The TfdR protein was capable of binding to the tfdC promoter region and activated tfdCDEF gene expression by a factor of 80 to 100 when provided in cis as a tfdR-tfdCDEF hybrid regulon. Although to a lesser extent, induction of tfdCDEF expression was also observed when no functional TfdR protein was provided, implying cross-activation by chromosomally encoded regulatory elements in R. eutropha JMP134(pJP4).

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Purification of the LysR family regulator, ClcR, and its interaction with the Pseudomonas putida clcABD chlorocatechol operon promoter

Cited by 33 publications

References 15 publications

Bacterial Transcriptional Regulators for Degradation Pathways of Aromatic Compounds

Bacterial Transcriptional Regulators for Degradation Pathways of Aromatic Compounds

Synergistic transcriptional activation by one regulatory protein in response to two metabolites

The tfdR gene product can successfully take over the role of the insertion element-inactivated TfdT protein as a transcriptional activator of the tfdCDEF gene cluster, which encodes chlorocatechol degradation in Ralstonia eutropha JMP134(pJP4)

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