Development of a Bacterial Biosensor for Nitrotoluenes: The Crystal Structure of the Transcriptional Regulator DntR

Смирнова, И. А.; Dian, Cyril; Leonard, Gordon A.; McSweeney, Seán; Birse, Darcy; Brzezinski, Peter

doi:10.1016/j.jmb.2004.04.071

Cited by 83 publications

(136 citation statements)

References 37 publications

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“…These include DntR isolated from Burkholderia spp., which regulates the expression of enzymes that are involved in catalysing the initial steps of the oxidative degradation of 2,4-dinitrotoluene (2,4-DNT) (Lönneberg et al, 2007). The crystal structure has been resolved to 2.6 Å (acetate at the co-inducer site) and 2.3 Å (thiocyanate at the co-inducer site) (Smirnova et al, 2004). These are not the physiological co-inducers for DntR, and studies have indicated that both sodium salicylate and 2,4-DNT are more likely to be the true co-inducers.…”

Section: Lysr Family Transcriptional Regulatorsmentioning

confidence: 99%

Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins

2008

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The LysR family of transcriptional regulators represents the most abundant type of transcriptional regulator in the prokaryotic kingdom. Members of this family have a conserved structure with an Nterminal DNA-binding helix-turn-helix motif and a C-terminal co-inducer-binding domain. Despite considerable conservation both structurally and functionally, LysR-type transcriptional regulators (LTTRs) regulate a diverse set of genes, including those involved in virulence, metabolism, quorum sensing and motility. Numerous structural and transcriptional studies of members of the LTTR family are helping to unravel a compelling paradigm that has evolved from the original observations and conclusions that were made about this family of transcriptional regulators.

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Section: Lysr Family Transcriptional Regulatorsmentioning

confidence: 99%

Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins

2008

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“…Effector binding occurs in a small cleft formed between RD-I and RD-II (Fig. 1) and is a hallmark of the LTTR family (22,(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80). A recent study using nondenaturing mass spectrometry has illustrated for the first time that an LTTR tetramer binds four molecules of its effector in a stepwise pattern while bound to DNA (81).…”

Section: Postranslational Regulation Of Cbbr Function: the Role Of Efmentioning

confidence: 99%

CbbR, the Master Regulator for Microbial Carbon Dioxide Fixation

Dangel

Tabita

2015

J Bacteriol

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Biological carbon dioxide fixation is an essential and crucial process catalyzed by both prokaryotic and eukaryotic organisms to allow ubiquitous atmospheric CO 2 to be reduced to usable forms of organic carbon. This process, especially the CalvinBassham-Benson (CBB) pathway of CO 2 fixation, provides the bulk of organic carbon found on earth. The enzyme ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RubisCO) performs the key and rate-limiting step whereby CO 2 is reduced and incorporated into a precursor organic metabolite. This is a highly regulated process in diverse organisms, with the expression of genes that comprise the CBB pathway (the cbb genes), including RubisCO, specifically controlled by the master transcriptional regulator protein CbbR. Many organisms have two or more cbb operons that either are regulated by a single CbbR or employ a specific CbbR for each cbb operon. CbbR family members are versatile and accommodate and bind many different effector metabolites that influence CbbR's ability to control cbb transcription. Moreover, two members of the CbbR family are further posttranslationally modified via interactions with other transcriptional regulator proteins from two-component regulatory systems, thus augmenting CbbR-dependent control and optimizing expression of specific cbb operons. In addition to interactions with small effector metabolites and other regulator proteins, CbbR proteins may be selected that are constitutively active and, in some instances, elevate the level of cbb expression relative to wild-type CbbR. Optimizing CbbR-dependent control is an important consideration for potentially using microbes to convert CO 2 to useful bioproducts.

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“…The structure of the full-length LysR-type regulator CbnR has been solved by X-ray crystallography ( Fig. 2) (342), as have the structures of the C-terminal domains of CysB, DntR, and OxyR (79,453,496). The N-terminal domain of CbnR consists of three helices and is followed by two ␤-strands, which are connected to the Cterminal domain by a long helix that mediates protein dimerization (Fig.…”

Section: Host Detection During Nodule Formationmentioning

confidence: 99%

Detection of and Response to Signals Involved in Host-Microbe Interactions by Plant-Associated Bacteria

Brencic

Winans

2005

Microbiol Mol Biol Rev

337

208

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Diverse interactions between hosts and microbes are initiated by the detection of host-released chemical signals. Detection of these signals leads to altered patterns of gene expression that culminate in specific and adaptive changes in bacterial physiology that are required for these associations. This concept was first demonstrated for the members of the family Rhizobiaceae and was later found to apply to many other plant-associated bacteria as well as to microbes that colonize human and animal hosts. The family Rhizobiaceae includes various genera of rhizobia as well as species of Agrobacterium. Rhizobia are symbionts of legumes, which fix nitrogen within root nodules, while Agrobacterium tumefaciens is a pathogen that causes crown gall tumors on a wide variety of plants. The plant-released signals that are recognized by these bacteria are low-molecular-weight, diffusible molecules and are detected by the bacteria through specific receptor proteins. Similar phenomena are observed with other plant pathogens, including Pseudomonas syringae, Ralstonia solanacearum, and Erwinia spp., although here the signals and signal receptors are not as well defined. In some cases, nutritional conditions such as iron limitation or the lack of nitrogen sources seem to provide a significant cue. While much has been learned about the process of host detection over the past 20 years, our knowledge is far from being complete. The complex nature of the plant-microbe interactions makes it extremely challenging to gain a comprehensive picture of host detection in natural environments, and thus many signals and signal recognition systems remain to be described

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Development of a Bacterial Biosensor for Nitrotoluenes: The Crystal Structure of the Transcriptional Regulator DntR

Cited by 83 publications

References 37 publications

Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins

Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins

CbbR, the Master Regulator for Microbial Carbon Dioxide Fixation

Detection of and Response to Signals Involved in Host-Microbe Interactions by Plant-Associated Bacteria

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