Reconstitution of the Rhodobacter sphaeroides cbb3-PrrBA Signal Transduction Pathway in Vitro

Oh, Jun-Hyok; Ko, In-Jeong; Kaplan, Samuel

doi:10.1021/bi0496440

Cited by 60 publications

(62 citation statements)

References 29 publications

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“…capsulatus, it has been proposed that reduction of cytochrome c oxidase activity in a senC mutant affects the oxidation/reduction state of the ubiquinone pool, leading to alteration of photosystem and respiratory gene expression (Swem et al, 2005). In Rhodobacter sphaeroides, SenC has been proposed to act as a signal mediator between cytochrome cbb 3 oxidase and a sensor kinase RegB that is involved in controlling expression of a number of processes, such as photosynthesis and respiration (Oh et al, 2004). Interaction of S. meliloti SenC with global regulation of this type could influence mobility.…”

Section: Discussionmentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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Section: Discussionmentioning

confidence: 99%

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

et al. 2007

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“…A mutation in the cytoplasmic loop between TM helix 2 and TM helix 3 causes constitutive (i.e., oxygen-insensitive) kinase activity in vivo (56). The aerobic respiratory chain has been shown to supply the signal by interaction of the cytochrome cbb 3 oxidase with PrrB/RegB (55,(191)(192)(193). In a defined in vitro system, cytochrome oxidase cbb 3 stimulated the phosphatase/kinase activity ratio of PrrB in the presence of O 2 , resulting in a decrease of PrrA-phosphate and thus of the active state of PrrA (193).…”

Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

“…The aerobic respiratory chain has been shown to supply the signal by interaction of the cytochrome cbb 3 oxidase with PrrB/RegB (55,(191)(192)(193). In a defined in vitro system, cytochrome oxidase cbb 3 stimulated the phosphatase/kinase activity ratio of PrrB in the presence of O 2 , resulting in a decrease of PrrA-phosphate and thus of the active state of PrrA (193). Sensing and optimal kinase activity required the TM sensing domain of PrrB.…”

Section: Regb/prrb-like Redox-responding Global Sensor Kinases With Smentioning

confidence: 99%

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Mascher

Helmann

Unden

2006

Microbiol Mol Biol Rev

625

652

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SUMMARY Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sensing. In order to gain insight into the mechanisms of stimulus perception by bacterial histidine kinases, we here survey sensor domain architecture and topology within the bacterial membrane, functional aspects related to this topology, and sequence and phylogenetic conservation. Based on these criteria, three groups of histidine kinases can be differentiated. (i) Periplasmic-sensing histidine kinases detect their stimuli (often small solutes) through an extracellular input domain. (ii) Histidine kinases with sensing mechanisms linked to the transmembrane regions detect stimuli (usually membrane-associated stimuli, such as ionic strength, osmolarity, turgor, or functional state of the cell envelope) via their membrane-spanning segments and sometimes via additional short extracellular loops. (iii) Cytoplasmic-sensing histidine kinases (either membrane anchored or soluble) detect cellular or diffusible signals reporting the metabolic or developmental state of the cell. This review provides an overview of mechanisms of stimulus perception for members of all three groups of bacterial signal-transducing histidine kinases.

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“…However, activity of the PrrB kinase depends on electron flow to the cbb 3 cytochrome c oxidase (36), which may be affected by the lower expression of the cco-rdx cluster (Fig. 1) and result in the lower activity of its cognate response regulator PrrA.…”

Section: Vol 187 2005mentioning

confidence: 99%

Transcriptome and Physiological Responses to Hydrogen Peroxide of the Facultatively Phototrophic Bacterium Rhodobacter sphaeroides

Zeller

Moskvin

et al. 2005

J Bacteriol

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The transcriptome responses to hydrogen peroxide, H 2 O 2 , of the facultatively phototrophic bacterium Rhodobacter sphaeroides grown under semiaerobic conditions were investigated. At 7 min after the addition of 1 mM H 2 O 2 , the expression of approximately 9% of all genes (total, 394) was changed reliably by at least twofold. At 30 min, the number of genes (total, 88) and the magnitude of expression changes were much lower, indicating rapid recovery from stress. Two types of responses were observed: (i) an H 2 O 2 stress response per se and (ii) a shift to high-oxygen metabolism. The former response involved the upregulation of genes for H 2 O 2 detoxification, protein folding and proteolysis, DNA damage repair, iron transport and storage, iron-sulfur cluster repair, and the downregulation of genes for protein translation, motility, and cell wall and lipopolysaccharide synthesis. The shift to high-oxygen metabolism was evident from the differential regulation of genes for aerobic electron transport chain components and the downregulation of tetrapyrrole biosynthesis and photosystem genes. The abundance of photosynthetic complexes was decreased upon prolonged exposure of R. sphaeroides to H 2 O 2 , thus confirming the physiological significance of the transcriptome data. The regulatory pathways mediating the shift to high-oxygen metabolism were investigated. They involved the anaerobic activator FnrL and the antirepressor-repressor AppA-PpsR system. The transcription of FnrL-dependent genes was down at 7 min, apparently due to the transient inactivation by H 2 O 2 of the iron-sulfur cluster of FnrL. The transcription of the AppA-PpsR-dependent genes was down at 30 min, apparently due to the significant decrease in appA mRNA.In natural environments, microorganisms have to cope with oxidative stress caused by reactive oxygen species (ROS). In aerobically growing bacteria, the autooxidation of the respiratory chain components is believed to be one of the main sources of endogenous ROS (16,20,30); however, additional sources exist (48). ROS are also produced by exposure of aerobically grown cells to metals, redox-active chemicals, or radiation. To cope with damage inflicted by ROS, bacteria induce oxidative stress defense systems. These include superoxide dismutases, catalases, and peroxidases directly involved in ROS detoxification and repair mechanisms. The ROS-oxidized cysteine and methionine residues of proteins are repaired (reduced) by the thioredoxin, glutathion/glutaredoxin, and methionine sulfoxide reductase systems. DNA is protected from damage by specific ROS-induced DNA-binding proteins, while damaged DNA is repaired via the SOS response (1, 8, 52).Rhodobacter sphaeroides is a facultatively phototrophic bacterium belonging to the alpha division of the proteobacteria that can use various pathways for energy generation. At high O 2 tension, it uses aerobic respiration and lacks photosynthetic complexes. When O 2 tension drops, the expression of the photosystem (PS) genes increases, resulting in the produ...

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Reconstitution of the Rhodobacter sphaeroides cbb₃-PrrBA Signal Transduction Pathway in Vitro

Cited by 60 publications

References 29 publications

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

Pleiotropic effects of mutations that alter the Sinorhizobium meliloti cytochrome c respiratory system

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Transcriptome and Physiological Responses to Hydrogen Peroxide of the Facultatively Phototrophic Bacterium Rhodobacter sphaeroides

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