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. 2021 Feb 22;12:1210. doi: 10.1038/s41467-021-21306-0

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a The model depicts the bidirectional and dynamic process of the cellular response to potassium limitation. When potassium becomes limiting, the diadenylate cyclases respond and produce less c-di-AMP and c-di-AMP receptor proteins are present in the apo-form. One apo-DarB dimer binds to Rel and by this disrupts the Rel dimer. This leads to formation of the DarB–Rel complex as suggested by the presented data. One DarB dimer is bound by two Rel monomers, one on each side. The interaction occurs via the HYD-SYN domains of Rel. Interaction of DarB with Rel leads to stimulation of (p)ppGpp synthesis. (p)ppGpp accumulation induces the stringent response and inhibits the c-di-AMP-degrading phosphodiesterases GdpP and PgpH. This leads to increasing intracellular c-di-AMP amounts. DarB can then bind c-di-AMP and is thus no longer able to interact with Rel. b The model shows the DarB-Rel complex as suggested by our data. One DarB dimer is bound by two Rel monomers, one on each side. The interaction occurs via the HYD-SYN domains of Rel. DarB, blue; Rel, gray. cdA, c-di-AMP; HYD, hydrolase domain; SYN, synthetase domain; TGS, TGS domain (for: ThrRS, GTPase, and SpoT); ZFD, Zinc finger domain; RRM, RNA Recognition Motif.