ATPase as a switch in P
            <sub>II</sub>
            signal transduction

Zhang, Cheng‐Cai; Zhou, Cong‐Zhao

doi:10.1073/pnas.1310926110

Cited by 4 publications

(8 citation statements)

References 9 publications

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“…We found that 2‐OG cannot effectively dissociate PII from PipX when the concentration of Mg 2+ ions is two‐fold or several fold below that of ATP. ATP, ADP and Mg‐ATP can all bind to PII . Our observation can thus be explained by a competition between ATP and Mg‐ATP for PII binding.…”

Section: Discussionmentioning

confidence: 64%

“…Several studies demonstrated that both ATP and Mg 2+ are essential for efficient 2‐OG binding to the PII protein . 2‐OG binds to PII in the vicinity of Mg‐ATP, with the Mg 2+ coordinating 2‐OG and ATP.…”

Section: Resultsmentioning

confidence: 99%

“…D); when the concentration of ATP increased to 5 or 10 m m , 2‐OG was unable to dissociate the protein complex, while a concentration of ATP of 2 m m gave an intermediate response of PROBS‐2 to 2‐OG. Both ATP and Mg‐ATP can bind to PII, but only the latter molecule allowed subsequent binding of 2‐OG . Thus, if the concentration of ATP is too high relative to that of Mg 2+ , such conditions favour the formation of PII bound with ATP rather than Mg‐ATP.…”

Section: Resultsmentioning

confidence: 99%

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Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

et al. 2014

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2-Oxoglutarate is a central metabolite and a signalling molecule in both prokaryotes and eukaryotes. The cellular levels of 2-oxoglutarate vary rapidly in response to environmental changes, but an easy and reliable approach is lacking for the measurement of 2-oxoglutarate. Here we report a biosensor of 2-oxoglutarate based on the 2-oxoglutarate-dependent dissociation of the PII-PipX protein complex from cyanobacteria. Fusions of PII and PipX to either cyan or yellow fluorescent protein can form a complex and their interaction can be detected by fluorescence resonance energy transfer (FRET). Mutations in PII or PipX that affect their interaction strongly decrease the FRET signal. Furthermore, the FRET signal is negatively affected, in a specific and concentration-dependent manner, by the presence of 2-oxoglutarate. This 2-oxoglutarate biosensor responds specifically and rapidly to a large range of 2-oxoglutarate levels and is highly robust under different conditions, including in bacterial cell extracts. We further used this biosensor to study the interaction between PII and its effectors, and our data indicate that excess of Mg 2+ ions is a key factor for PII to respond efficiently to an increase in 2-oxoglutarate levels. This study paves the way for probing the dynamics of 2-oxoglutarate in various organisms and provides a valuable tool for the understanding of the molecular mechanism in metabolic regulation. Structured digital abstractPipX binds to PII by fluorescent resonance energy transfer (1, 2, 3)

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Section: Discussionmentioning

confidence: 64%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

et al. 2014

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“…Transcript abundances for the nitrogen regulatory protein P II gene, glnK , were also higher on non–limiting ammonium. The most recent mechanistic insight into the signaling role of the P II protein suggests that a post translational change driven by changes in its observed ATPase activity under fluctuating nitrogen levels sensed by intracellular α–KG would facilitate or inhibit ammonium uptake through the ammonium transporter channel 22 . The glnK gene can be located upstream and downstream of amtB .…”

Section: Discussionmentioning

confidence: 99%

Metabolic networks for nitrogen utilization in Prevotella ruminicola 23

Kim

Méndez–García

Geier

et al. 2017

Sci Rep

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Nitrogen metabolism in gut systems remains poorly studied in spite of its importance for microbial growth and its implications for the metabolism of the host. Prevotella spp. are the most predominant bacteria detected in the rumen, but their presence has also been related to health and disease states in the human gut and oral cavity. To explore the metabolic networks for nitrogen assimilation in this bacterium, changes in gene expression profiles in response to variations in the available nitrogen source and to different concentrations of ammonium were analyzed by microarray and reverse transcription quantitative PCR, and linked with function by further proteomic analysis. The observed patterns of transcript abundances for genes involved in ammonium assimilation differed from the classical “enteric paradigm” for nitrogen utilization. Expression of genes encoding high substrate affinity nitrogen assimilation enzymes (GS-GOGAT system) was similar in growth-limiting and non-limiting nitrogen concentrations in P. ruminicola 23, whereas E. coli and Salmonella spp. responses to excess nitrogen involve only low substrate affinity enzymes. This versatile behavior might be a key feature for ecological success in habitats such as the rumen and human colon where nitrogen is rarely limiting for growth, and might be linked to previously reported Prevotella spp. population imbalances relative to other bacterial species in gut systems.

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“…We found that 2-OG cannot effectively dissociate PII from PipX when the concentration of Mg 2+ ions is two-fold or several fold below that of ATP. ATP, ADP and Mg-ATP can all bind to PII [10,31]. Our observation can thus be explained by a competition between ATP and Mg-ATP for PII binding.…”

mentioning

confidence: 60%

Fluorescence Resonance Energy Transfer Based on Interaction of PII and PipX Proteins Provides a Robust and Specific Biosensor for 2-Oxoglutarate, a Central Metabolite and a Signaling Molecule

Chen

Bernard

Hubert

et al. 2013

FEBS J

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ATPase as a switch in P _II signal transduction

Cited by 4 publications

References 9 publications

Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

Metabolic networks for nitrogen utilization in Prevotella ruminicola 23

Fluorescence Resonance Energy Transfer Based on Interaction of PII and PipX Proteins Provides a Robust and Specific Biosensor for 2-Oxoglutarate, a Central Metabolite and a Signaling Molecule

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ATPase as a switch in P II signal transduction

Cited by 4 publications

References 9 publications

Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

Fluorescence resonance energy transfer based on interaction of PII and PipX proteins provides a robust and specific biosensor for 2‐oxoglutarate, a central metabolite and a signalling molecule

Metabolic networks for nitrogen utilization in Prevotella ruminicola 23

Fluorescence Resonance Energy Transfer Based on Interaction of PII and PipX Proteins Provides a Robust and Specific Biosensor for 2-Oxoglutarate, a Central Metabolite and a Signaling Molecule

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ATPase as a switch in P _II signal transduction