ADP reduces the oxygen-binding affinity of a sensory histidine kinase, FixL: The possibility of an enhanced reciprocating kinase reaction

Nakamura, H.; Kumita, Hideyuki; Imai, Katsunori; Iizuka, Tetsutarō; Shiro, Yoshitsugu

doi:10.1073/pnas.0305795101

Cited by 31 publications

(27 citation statements)

References 39 publications

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“…SmFixL is known to self associate and to form a heterotetramer with FixJ. While there is reason to suggest that there is transphosphorylation of the kinase domains within the heterotetramer [42], this functional intimacy does not appear to support cooperative O 2 binding [33,43].…”

Section: Coordination Environmentmentioning

confidence: 91%

“…A recent study has provided compelling evidence that the heterotetramer (FixL) 2 (FixJ) 2 is mechanistically relevant due to intermolecular allosteric effects [43]. It was shown that ADP is an allosteric effector for negative feedback control of the O 2 affinity of the heme domain, which translates to positive allosteric regulation of kinase activity.…”

Section: Role Of Fixl Associationmentioning

confidence: 99%

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Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

Rodgers

Lukat-Rodgers

2005

Journal of Inorganic Biochemistry

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Section: Coordination Environmentmentioning

confidence: 91%

Section: Role Of Fixl Associationmentioning

confidence: 99%

Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

Rodgers

Lukat-Rodgers

2005

Journal of Inorganic Biochemistry

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“…Hemebinding proteins, recombinantly produced in E. coli, copurify with heme and show characteristic absorption peaks between 400 and 600 nm (26). Spectral analysis of purified and active TodS showed no maximum peaks in this wavelength range, indicating that it is unlikely that TodS exhibits a heme group.…”

Section: Discussionmentioning

confidence: 99%

The TodS–TodT two-component regulatory system recognizes a wide range of effectors and works with DNA-bending proteins

Lacal

Büsch

Guazzaroni

et al. 2006

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

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The TodS and TodT proteins form a previously unrecognized and highly specific two-component regulatory system in which the TodS sensor protein contains two input domains, each of which are coupled to a histidine kinase domain. This system regulates the expression of the genes involved in the degradation of toluene, benzene, and ethylbenzene through the toluene dioxygenase pathway. In contrast to the narrow substrate range of this catabolic pathway, the TodS effector profile is broad. TodS has basal autophosphorylation activity in vitro, which is enhanced by the presence of effectors. Toluene binds to TodS with high affinity (K d ‫؍‬ 684 ؎ 13 nM) and 1:1 stoichiometry. The analysis of the truncated variants of TodS reveals that toluene binds to the N-terminal input domain (K d ‫؍‬ 2.3 ؎ 0.1 M) but not to the C-terminal half. TodS transphosphorylates TodT, which binds to two highly similar DNA binding sites at base pairs ؊107 and ؊85 of the promoter. Integration host factor (IHF) plays a crucial role in the activation process and binds between the upstream TodT boxes and the ؊10 hexamer region. In an IHF-deficient background, expression from the tod promoter drops 8-fold. In vitro transcription assays confirmed the role determined in vivo for TodS, TodT, and IHF. A functional model is presented in which IHF favors the contact between the TodT activator, bound further upstream, and the ␣-subunit of RNA polymerase bound to the downstream promoter element. Once these contacts are established, the tod operon is efficiently transcribed.Pseudomonas ͉ sensor kinase ͉ toluene dioxygenase ͉ transcriptional regulator M any Pseudomonas putida strains are able to use benzene, toluene, and ethylbenzene as the sole carbon and energy source through the toluene dioxygenase (TOD) pathway (1). In this pathway, the aromatic hydrocarbons are oxidized to their corresponding substituted catechols, which are further metabolized to Krebs cycle intermediates (1, 2). The catabolic genes of the TOD pathway form the operon todXFC1C2BADEGIH, which is transcribed from a single promoter called P todX , located upstream from the todX gene (1-3). The todST genes are found downstream and form an independent operon that is expressed constitutively (2, 3).TodS and TodT have been proposed to form a two-component regulatory system (TCS) that regulates the tod catabolic operon in P. putida F1 (3). TodT shows all of the characteristics of a response regulator, whereas sequence-based domain predictions indicate that the 108-kDa TodS belongs to a family of sensor histidine kinases that have not been studied at the biochemical level. TodS is predicted to comprise two supradomains, each containing a PAS͞PAC sensory domain and a histidine kinase domain. The supradomains are separated by the receiver domain of a response regulator. In contrast to other histidine kinases, TodS apparently lacks transmembrane regions (3). The mode of action of this previously unrecognized type of histidine kinase has yet to be established. On the basis of moderate sequence simil...

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“…In the root nodule bacteria, Rhizobium meliloti and Bradyrhizobium japonicum, FixLs with a heme-containing PAS domain regulate the expres-sion of genes involved in nitrogen fixation and the anaerobic respiratory chain (11,13). DevS (DosS) and DosT, containing a heme-bound GAF domain, regulate entry of the pathogenic bacterium, Mycobacterium tuberculosis, into dormancy (14 -17).…”

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confidence: 99%

Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5

Kitanishi

Kobayashi

Uchida

et al. 2011

Journal of Biological Chemistry

108

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Two-component signal transduction systems regulate numerous important physiological functions in bacteria. In this study we have identified, cloned, overexpressed, and characterized a dimeric full-length heme-bound (heme:protein, 1:1 stoichiometry) globin-coupled histidine kinase (AfGcHK) from Anaeromyxobacter sp. strain Fw109-5 for the first time. The Fe(III), Fe(II)-O2, and Fe(II)-CO complexes of the protein displayed autophosphorylation activity, whereas the Fe(II) complex had no significant activity. A H99A mutant lost heme binding ability, suggesting that this residue is the heme proximal ligand. Moreover, His-183 was proposed as the autophosphorylation site based on the finding that the H183A mutant protein was not phosphorylated. The phosphate group of autophosphorylated AfGcHK was transferred to Asp-52 and Asp-169 of a response regulator, as confirmed from site-directed mutagenesis experiments. Based on the amino acid sequences and crystal structures of other globin-coupled oxygen sensor enzymes, Tyr-45 was assumed to be the O2 binding site at the heme distal side. The O2 dissociation rate constant, 0.10 s−1, was substantially increased up to 8.0 s−1 upon Y45L mutation. The resonance Raman frequencies representing νFe-O2 (559 cm−1) and νO-O (1149 cm−1) of the Fe(II)-O2 complex of Y45F mutant AfGcHK were distinct from those of the wild-type protein (νFe-O2, 557 cm−1; νO-O, 1141 cm−1), supporting the proposal that Tyr-45 is located at the distal side and forms hydrogen bonds with the oxygen molecule bound to the Fe(II) complex. Thus, we have successfully identified and characterized a novel heme-based globin-coupled oxygen sensor histidine kinase, AfGcHK, in this study.

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ADP reduces the oxygen-binding affinity of a sensory histidine kinase, FixL: The possibility of an enhanced reciprocating kinase reaction

Cited by 31 publications

References 39 publications

Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

Insights into heme-based O2 sensing from structure–function relationships in the FixL proteins

The TodS–TodT two-component regulatory system recognizes a wide range of effectors and works with DNA-bending proteins

Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5

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