Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation

Dubey, Badri N.; Agustoni, Elia; Böhm, Raphael; Kaczmarczyk, Andreas; Mangia, Francesca; Arx, C. von; Jenal, Urs; Hiller, Sebastian; Plaza-Menacho, Iván; Schirmer, Tilman

doi:10.1101/675454

Cited by 2 publications

(2 citation statements)

References 40 publications

(53 reference statements)

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“…To date, the prototypical homodimeric transmembrane SHKs have eluded structural elucidation at full length. Certain noncanonical SHKs aside, structural information at (or, near) full length is only available for VicK from Streptococcus mutans and for the engineered LOV histidine kinase YF1 in its dark‐adapted, kinase‐active K state . Within both receptors, the sensor module comprises a PAS/LOV homodimer that connects to the effector module via a short coiled coil.…”

Section: Signal Transmission Through α‐Helical Bundles and Linkersmentioning

confidence: 99%

“…As visible light penetrates cell walls and membranes, most photoreceptor classes, and in particular LOV and BPhy receptors, are cytosolic, soluble proteins which greatly facilitates structural, biophysical, and mechanistic studies, even in the context of the full-length receptor. Conversely, with certain exceptions, 26 light-inert SHKs are predominantly transmembrane proteins that decode extracellular or periplasmic inputs into intracellular output. To date, transmembrane SHKs have eluded structure determination at full length.…”

Section: Photoreceptor Histidine Kinasesmentioning

confidence: 99%

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Signal transduction in photoreceptor histidine kinases

Möglich

2019

Protein Science

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Two‐component systems (TCS) constitute the predominant means by which prokaryotes read out and adapt to their environment. Canonical TCSs comprise a sensor histidine kinase (SHK), usually a transmembrane receptor, and a response regulator (RR). In signal‐dependent manner, the SHK autophosphorylates and in turn transfers the phosphoryl group to the RR which then elicits downstream responses, often in form of altered gene expression. SHKs also catalyze the hydrolysis of the phospho‐RR, hence, tightly adjusting the overall degree of RR phosphorylation. Photoreceptor histidine kinases are a subset of mostly soluble, cytosolic SHKs that sense light in the near‐ultraviolet to near‐infrared spectral range. Owing to their experimental tractability, photoreceptor histidine kinases serve as paradigms and provide unusually detailed molecular insight into signal detection, decoding, and regulation of SHK activity. The synthesis of recent results on receptors with light‐oxygen‐voltage, bacteriophytochrome and microbial rhodopsin sensor units identifies recurring, joint signaling strategies. Light signals are initially absorbed by the sensor module and converted into subtle rearrangements of α helices, mostly through pivoting and rotation. These conformational transitions propagate through parallel coiled‐coil linkers to the effector unit as changes in left‐handed superhelical winding. Within the effector, subtle conformations are triggered that modulate the solvent accessibility of residues engaged in the kinase and phosphatase activities. Taken together, a consistent view of the entire trajectory from signal detection to regulation of output emerges. The underlying allosteric mechanisms could widely apply to TCS signaling in general.

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Section: Signal Transmission Through α‐Helical Bundles and Linkersmentioning

confidence: 99%

Section: Photoreceptor Histidine Kinasesmentioning

confidence: 99%

Signal transduction in photoreceptor histidine kinases

Möglich

2019

Protein Science

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Precise transcription timing by a second-messenger drives a bacterial G1/S cell cycle transition

Kaczmarczyk

Hempel

Arx

et al. 2019

Preprint

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29Bacteria adapt their growth rate to their metabolic status and environmental 30 conditions by modulating the length of their quiescent G1 period. But the molecular 31 mechanisms controlling G1 length and exit from G1 are poorly understood. Here we 32 identify a key role for the second messenger c-di-GMP, and demonstrate that a gradual 33 increase in c-di-GMP concentration determines precise gene expression during G1/S in 34 Caulobacter crescentus. We show that c-di-GMP strongly stimulates the kinase ShkA, 35activates the TacA transcription factor, and initiates a G1/S-specific transcription 36 program leading to cell morphogenesis and S-phase entry. C-di-GMP activates ShkA by 37 binding to its central pseudo-receiver domain uncovering this wide-spread domain as a 38 novel signal input module of bacterial kinases. Activation of the ShkA-dependent 39 genetic program also causes c-di-GMP to reach peak levels, which triggers S-phase 40 entry and, in parallel, promotes proteolysis of ShkA and TacA. Thus, a gradual 41 increase of c-di-GMP results in a precisely tuned ShkA-TacA activity window enabling 42 G1/S specific gene expression before cells commit to replication initiation. By defining 43 a regulatory mechanism for G1/S control, this study contributes to understanding 44 bacterial growth control at the molecular level. cell division (D or G2) 1 . Since chromosome replication and cell division (C and D 49 periods) remain constant over a wide range of growth rates 2,3 , the step committing 50 cells to initiate chromosome replication largely determines bacterial proliferation rates. 51Bacteria like Escherichia coli or Bacillus subtilis can increase their growth rate by 52 bypassing the B period and by initiating replication multiple times per division cycle 2 . 53In contrast, Caulobacter crescentus strictly separates its cell cycle stages. An 54 asymmetric division generates a sessile stalked (ST) cell, which directly re-enters S-55 phase, and a motile swarmer (SW) cell that remains in G1 for a variable time 56 depending on nutrient availability 4,5 . Coincident with G1/S transition, motile SW cells 57 undergo morphogenesis to gain sessility ( Fig. 1a). But what determines the length of 58 G1 in this organism has remained unclear. 59In C. crescentus, replication initiation is regulated by the cell cycle kinase CckA. 60CckA is a bifunctional enzyme that acts as a kinase for the replication initiation 61 inhibitor CtrA in G1, but switches to being a phosphatase in S phase, resulting in the 62 inactivation of CtrA and clearance of the replication block 6 (Fig. 1a). The CckA switch 63 is governed by two response regulators, DivK and PleD. While DivK controls CckA 64 activity through protein-protein interactions 7-9 , PleD is a diguanylate cyclase, which is 65 responsible for the characteristic oscillation of c-di-GMP during the cell cycle 10 . The 66 concentration of c-di-GMP, below the detection limit in G1, increases during G1/S to 67 reach peak levels at the onset of S-phase 11 where it allosterically stimulates Cc...

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Hybrid histidine kinase activation by cyclic di-GMP-mediated domain liberation

Cited by 2 publications

References 40 publications

Signal transduction in photoreceptor histidine kinases

Signal transduction in photoreceptor histidine kinases

Precise transcription timing by a second-messenger drives a bacterial G1/S cell cycle transition

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