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. 2018 Nov 29;47(2):843–854. doi: 10.1093/nar/gky1201

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — EIIA^Ntr∼P binds the ACT domain of SpoT and inhibits its hydrolase activity. Upon nitrogen starvation (i.e. glutamine deprivation), EI^Ntr phosphorylates its downstream components, HPr and EIIA^Ntr. As a consequence, EIIA^Ntr∼P interacts with ACT to likely inhibit its stimulating effect on the hydrolase activity of SpoT. This inhibition avoids to degrade (p)ppGpp produced by the SD, this latter being strongly stimulated by HPr∼P by an unknown mechanism. In addition, increasing the (p)ppGpp level promotes the accumulation of the SpoT protein by a positive feedback loop mechanism on transcription of the spoT gene. Ultimately, the burst of (p)ppGpp delays the G1-to-S transition of C. crescentus (left) and S. meliloti (right) cells.