Erratum for Lori et al., “A Single-Domain Response Regulator Functions as an Integrating Hub To Coordinate General Stress Response and Development in Alphaproteobacteria”

Lori, Christian; Kaczmarczyk, Andreas; Jong, I. de; Jenal, Urs

doi:10.1128/mbio.01534-18

Cited by 9 publications

(1 citation statement)

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“…The KaiC‐associated histidine kinases might directly phosphorylate (or dephosphorylate) unidentified DNA‐binding transcriptional regulators in a KaiC‐dependent manner, by being spatially sequestered or activated/deactivated when bound to KaiC. Likewise, single‐domain response regulators can be used as phosphoryl sink or source within phosphotransfer networks and indirectly influence the phosphorylation state of multiple players, including transcriptional regulators (Lori et al, 2018). In Pseudomonas species, a number of phosphorylatable response regulators, like CbrB, CfcR, or GacA, are involved both in stress resistance and biofilm formation (Huertas‐Rosales et al, 2017; Monteagudo‐Cascales et al, 2022; Tagua et al, 2022) and could be indirectly affected by KaiC‐mediated phosphoryl rerouting.…”

Section: Discussionmentioning

confidence: 99%

KaiC‐like proteins contribute to stress resistance and biofilm formation in environmental Pseudomonas species

Terrettaz

Cabete

Geiser

et al. 2023

Environmental Microbiology

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KaiC is the central cog of the circadian clock in Cyanobacteria. Close homologues of this protein are widespread among nonphotosynthetic bacteria, but the function, interaction network, and mechanism of action of these proteins are still largely unknown. Here, we focus on KaiC homologues found in environmental Pseudomonas species. Using bioinformatics, we describe the distribution of this protein family in the genus and reveal a conserved interaction network comprising a histidine kinase and response regulator. We characterize experimentally the only KaiC homologue present in Pseudomonas putida KT2440 and Pseudomonas protegens CHA0. Through phenotypic assays and transcriptomics, we show that KaiC is involved in osmotic and oxidative stress resistance in P. putida and in biofilm production in both species. KaiC homologues are found in different phosphorylation states and physically interact with a cognate histidine kinase and response regulator. In contrast with cyanobacterial counterparts, the expression and phosphorylation of KaiC homologues do not correlate with light variations under 12:12 light: dark cycles in either Pseudomonas species, and KaiC itself is not required to support a light‐driven behaviour in P. putida. Overall, this suggests that KaiC homologues in Pseudomonas species are involved in environmental stress resistance but not in responses to diurnal rhythms.

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Section: Discussionmentioning

confidence: 99%

KaiC‐like proteins contribute to stress resistance and biofilm formation in environmental Pseudomonas species

Terrettaz

Cabete

Geiser

et al. 2023

Environmental Microbiology

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Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter

et al. 2020

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Bacteria adapt their growth rate to their metabolic status and environmental conditions by modulating the length of their G1 period. Here we demonstrate that a gradual increase in the concentration of the second messenger c-di-GMP determines precise gene expression during G1/S transition in Caulobacter crescentus. We show that c-di-GMP stimulates the kinase ShkA by binding to its central pseudo-receiver domain, activates the TacA transcription factor, and initiates a G1/S-specific transcription program leading to cell morphogenesis and S-phase entry. Activation of the ShkA-dependent genetic program causes c-di-GMP to reach peak levels, which triggers S-phase entry and promotes proteolysis of ShkA and TacA. Thus, a gradual increase of c-di-GMP results in precise control of ShkA-TacA activity, enabling G1/Sspecific gene expression that coordinates cell cycle and morphogenesis.

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Regulation of bacterial cell cycle progression by redundant phosphatases

Coppine

Kaczmarczyk

Petit

et al. 2020

Preprint

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In the model organism Caulobacter crescentus, a network of two-component systems involving the response regulators CtrA, DivK and PleD coordinate cell cycle progression with differentiation. Active phosphorylated CtrA prevents chromosome replication in G1 cells while simultaneously regulating expression of genes required for morphogenesis and development. At the G1-S transition, phosphorylated DivK (DivK~P) and PleD (PleD~P) accumulate to indirectly inactivate CtrA, which triggers DNA replication initiation and concomitant cellular differentiation. The phosphatase PleC plays a pivotal role in this developmental program by keeping DivK and PleD phosphorylation levels low during G1, thereby preventing premature CtrA inactivation. Here, we describe CckN as a second phosphatase akin to PleC that dephosphorylates DivK~P and PleD~P in G1 cells. However, in contrast to PleC, we do not detect kinase activity with CckN. The effects of CckN inactivation are largely masked when PleC is present, but become evident when PleC and DivJ, the major kinase for DivK and PleD, are absent. Accordingly, mild overexpression of cckN restores most phenotypic defects of a pleC null mutant. We also show that CckN and PleC are proteolytically degraded in a ClpXP-dependent way well before the onset of the S phase. Surprisingly, known ClpX adaptors are dispensable for PleC and CckN proteolysis, suggesting the existence of adaptors specifically involved in proteolytic removal of cell cycle regulators. Since cckN expression is induced in stationary phase, depending on the stress alarmone (p)ppGpp, we propose that CckN acts as an auxiliary factor responding to environmental stimuli to modulate CtrA activity under suboptimal conditions.ImportanceTwo-component signal transduction systems are widely used by bacteria to sense environmental signals and respond accordingly by modulating various cellular processes, such as cell cycle progression. In Caulobacter crescentus, PleC acts as a phosphatase that indirectly protects the response regulator CtrA from premature inactivation during the G1 phase of the cell cycle. Here, we provide genetic and biochemical evidence that PleC is seconded by another phosphatase, CckN. The activity of PleC and CckN phosphatases is restricted to G1 phase since both proteins are timely degraded by proteolysis just before the G1-S transition. This degradation requires new proteolytic adaptors as well as an unsuspected N-terminal motif for CckN. Our work illustrates a typical example of redundant functions between two-component proteins.

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Erratum for Lori et al., “A Single-Domain Response Regulator Functions as an Integrating Hub To Coordinate General Stress Response and Development in Alphaproteobacteria”

Cited by 9 publications

References 0 publications

KaiC‐like proteins contribute to stress resistance and biofilm formation in environmental Pseudomonas species

KaiC‐like proteins contribute to stress resistance and biofilm formation in environmental Pseudomonas species

Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter

Regulation of bacterial cell cycle progression by redundant phosphatases

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