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- W3184017385 abstract "Bacteria regulate their metabolism to adapt and survive adverse conditions, in particular to stressful downshifts in nutrient availability. These shifts trigger the so-called stringent response, coordinated by the signaling molecules guanosine tetra and pentaphosphate collectively referred to as (p)ppGpp. In Escherichia coli , accumulation of theses alarmones depends on the (p)ppGpp synthetase RelA and the bifunctional (p)ppGpp synthetase/hydrolase SpoT. A tight regulation of these intracellular activities is therefore crucial to rapidly adjust the (p)ppGpp levels in response to environmental stresses but also to avoid toxic consequences of (p)ppGpp over-accumulation. In this study, we show that the small protein NirD restrains RelA-dependent accumulation of (p)ppGpp and can inhibit the stringent response in E. coli . Mechanistically, our in vivo and in vitro studies reveal that NirD directly binds the catalytic domains of RelA to balance (p)ppGpp accumulation. Finally, we show that NirD can control RelA activity by directly inhibiting the rate of (p)ppGpp synthesis." @default.
- W3184017385 created "2021-08-02" @default.
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- W3184017385 date "2021-07-29" @default.
- W3184017385 modified "2023-10-17" @default.
- W3184017385 title "NirD curtails the stringent response by inhibiting RelA activity in Escherichia coli" @default.
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- W3184017385 doi "https://doi.org/10.7554/elife.64092" @default.
- W3184017385 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8321558" @default.
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- W3184017385 hasPublicationYear "2021" @default.
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