Structure of the Full-Length Bacteriophytochrome from the Plant Pathogen Xanthomonas campestris Provides Clues to its Long-Range Signaling Mechanism

Otero, Lisandro H.; Klinke, S.; Rinaldi, Jimena; Escobar, Francisco Velázquez; Mroginski, María Andrea; López, María Fernández; Malamud, Florencia; Vojnov, Adrián Alberto; Hildebrandt, Peter; Goldbaum, Fernando A.; Bonomi, Hernán Ruy

doi:10.1016/j.jmb.2016.04.012

Cited by 70 publications

(150 citation statements)

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“…( A ) Superposition of PSM modules from different published phytochrome structures featuring a parallel dimeric assembly to Is PadC (cyan) revealed almost identical arrangements of the PAS-GAF bidomain [root mean square deviation (RMSD) of 1.5, 1.2, 1.0, 0.9, and 0.9 Å for Protein Data Bank (PDB) 4OUR_B (blue) ( 60 ), 3G6O_A (violet) ( 16 ), 4Q0J_A (orange) ( 61 ), 5AKP_B (green) ( 26 ), and 5C5K_B (red) ( 20 ), respectively]. Irrespective of the β-hairpin or α-helical character of the tongue region, the PHY domains cluster in similar positions relative to the PAS-GAF domains.…”

Section: Resultsmentioning

confidence: 99%

Long-range allosteric signaling in red light–regulated diguanylyl cyclases

et al. 2017

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Section: Resultsmentioning

confidence: 99%

Long-range allosteric signaling in red light–regulated diguanylyl cyclases

et al. 2017

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“…As the PCMs have mostly been structurally elucidated as truncated proteins without attached effector modules, the observed quaternary structure need not necessarily correspond to the one in the full‐length receptor. The parallel arrangement appears physiologically more relevant as it is supported by structural data on BPhys with attached effector modules and by the parallel homodimeric nature of the most common BPhy effector modules, see above. Notably, the architecture of the parallel PCM homodimer is reminiscent of the LOV‐SHK architecture that also features parallel homodimers, α‐helical interface and laterally suspended globular sensor domains of the PAS superfamily.…”

Section: Photosensory Inputmentioning

confidence: 87%

“…With but few exceptions, the PCMs have been structurally elucidated in isolation, that is, as PAS‐GAF‐PHY constructs without covalently attached C‐terminal effector module. Where present in the structure, the effectors are mostly connected to the PCM via a continuous parallel coiled coil, thus possibly restricting the quaternary structures the PCM can adopt in the Pr and Pfr states. In particular, it remains to be seen whether the large‐scale splaying apart of the PHY domains observed for the isolated Dr BPhy PCM manifests to the same extent within the context of full‐length native and engineered BPhy receptors .…”

Section: Photosensory Inputmentioning

confidence: 99%

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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“…In addition to the photoinduced conversions, there is a thermal pathway between the parent states. Except for a phytochrome from Xanthomonas campestris for which these transformations proceed in both directions to a detectable extent, thermal Pr/Pfr conversions are essentially unidirectional such that the Pr and Pfr state are the stable (“dark”) states in prototypical and bathy phytochromes, respectively (Figure ). In this work, however, we provided evidence for an additional thermal recovery route of the dark state via the Meta intermediate which competes with the final step of the respective photoconversion (Figure ).…”

Section: Figurementioning

confidence: 99%

The Photoconversion of Phytochrome Includes an Unproductive Shunt Reaction Pathway

et al. 2018

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Phytochromes are modular bimodal photoswitches that control gene expression for morphogenetic processes in plants. These functions are triggered by photoinduced conversions between the inactive and active states of the photosensory module, denoted as Pr and Pfr, respectively. In the present time-resolved resonance Raman spectroscopic study of bacterial representatives of this photoreceptor family, we demonstrate that these phototransformations do not represent linear processes but include a branching reaction back to the initial state, prior to (de)activation of the output module. Thus, only a fraction of the photoreceptors undergoing the phototransformations can initiate the downstream signaling process, consistent with phytochrome's function as a sensor for more durable changes of light conditions.

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Structure of the Full-Length Bacteriophytochrome from the Plant Pathogen Xanthomonas campestris Provides Clues to its Long-Range Signaling Mechanism

Cited by 70 publications

References 69 publications

Long-range allosteric signaling in red light–regulated diguanylyl cyclases

Long-range allosteric signaling in red light–regulated diguanylyl cyclases

Signal transduction in photoreceptor histidine kinases

The Photoconversion of Phytochrome Includes an Unproductive Shunt Reaction Pathway

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