HAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor Kinase

Matamouros, Susana; Hager, Kyle R.; Miller, Samuel I.

doi:10.1128/mbio.00616-15

Cited by 43 publications

(58 citation statements)

References 59 publications

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“…It has been suggested that the HAMP domain regulates the phosphorylation of homodimeric sensor proteins by transmitting the conformational changes in the ligand-binding domains to the C-terminal signaling kinase domains (Aravind and Ponting, 1999; Klose et al, 2014; Schultz et al, 2015). This model is supported by genetic and biochemical studies (Zhou et al, 2009; Matamouros et al, 2015). …”

Section: Fungal Histidine Kinases Linked To Phenylpyrrole Resistancementioning

confidence: 69%

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Kilani¹,

Fillinger²

2016

Front. Microbiol.

106

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Phenylpyrroles are chemical analogs of the natural antifungal compound pyrrolnitrin. Fenpiclonil, but mainly fludioxonil are registered against multiple fungal crop diseases since over 25 years for seed or foliar treatment. They have severe physiological impacts on the pathogen, including membrane hyperpolarization, changes in carbon metabolism and the accumulation of metabolites leading to hyphal swelling and burst. The selection and characterization of mutants resistant to phenylpyrroles have revealed that these fungicides activate the fungal osmotic signal transduction pathway through their perception by a typical fungal hybrid histidine kinase (HHK). The HHK is prone to point mutations that confer fungicide resistance and affect its sensor domain, composed of tandem repeats of HAMP motifs. Fludioxonil resistant mutants have been selected in many fungal species under laboratory conditions. Generally they present severe impacts on fitness parameters. Since only few cases of field resistance specific to phenylpyrroles have been reported one may suspect that the fitness penalty of phenylpyrrole resistance is the reason for the lack of field resistance.

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Section: Fungal Histidine Kinases Linked To Phenylpyrrole Resistancementioning

confidence: 69%

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Kilani¹,

Fillinger²

2016

Front. Microbiol.

106

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“…We therefore propose that distinct conformational inputs result from binding of cognate AIPs to the sensor domains of each AgrC subgroup. Testing this idea will require additional biochemical study, perhaps involving crosslinking approaches (Matamouros et al, 2015; Molnar et al, 2014; Saita et al, 2015; Wang et al, 2014), although high-resolution structural information on the system will ultimately be needed to fully understand these inputs.…”

Section: Discussionmentioning

confidence: 99%

Functional Plasticity of the AgrC Receptor Histidine Kinase Required for Staphylococcal Virulence

Wang

Zhao

Xie

et al. 2017

Cell Chemical Biology

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Summary Staphylococcus aureus employs the receptor histidine kinase (RHK), AgrC, to detect quorum-sensing (QS) pheromones, the autoinducer peptides (AIPs), which regulate the virulence of the bacterium. Variation in the QS circuit divides S. aureus into four subgroups, each producing a specific AIP-AgrC pair. While the timing of QS induction is known to differ among these subgroups, the molecular basis of this phenomenon is unknown. Here we report the successful reconstitution of several AgrC variants and show that the agonist induced activity of the receptors varies in a manner that accounts for these temporal differences in QS induction. Our studies also reveal a key regulatory hotspot on AgrC that controls the basal activity of RHK as well as the responsiveness of the system to ligand inputs. Collectively, these studies offer insights into the capacity of the RHK for adaptive evolution.

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“…Support for functionally relevant changes in helical supercoiling within the coiled‐coil linker derives from both biochemical data and structural analyses. In several systems, sequence and length variations of the linker implied its coiled‐coil structure and signal‐dependent changes in α‐helical supercoiling . For the present scope, ample data on the blue‐light‐responsive LOV histidine kinase YF1 are most relevant .…”

Section: Signal Transmission Through α‐Helical Bundles and Linkersmentioning

confidence: 90%

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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HAMP Domain Rotation and Tilting Movements Associated with Signal Transduction in the PhoQ Sensor Kinase

Cited by 43 publications

References 59 publications

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Phenylpyrroles: 30 Years, Two Molecules and (Nearly) No Resistance

Functional Plasticity of the AgrC Receptor Histidine Kinase Required for Staphylococcal Virulence

Signal transduction in photoreceptor histidine kinases

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