Phytochromes from <i>Agrobacterium fabrum</i>

Lamparter, Tilman; Krauß, Norbert; Scheerer, Patrick

doi:10.1111/php.12761

Cited by 25 publications

(27 citation statements)

References 106 publications

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“…Blue light sensing using FAD (BLUF) domain-containing receptors present in bacteria and some algae has also been implicated in temperature sensing (Nakasone et al, 2010). Bacterial phytochromes have been proposed to sense light and temperature (Lamparter et al, 2017).…”

Section: Reviewmentioning

confidence: 99%

Light and temperature cues: multitasking receptors and transcriptional integrators

Casal

Qüesta

2017

New Phytologist

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Contents Summary1029I.Introduction1029II.Convergence at the receptor1030III.Convergence at transcriptional hubs1031IV.Convergence involving clock components1033V.Conclusions1033Acknowledgements1033References1033 Summary The combined information provided by light and temperature cues helps to optimise plant body architecture and physiology. Plants possess elaborate systems to sense and respond to these stimuli. Simultaneous perception of light and temperature by dual receptors such as phytochrome B and phototropin leads to immediate signalling convergence. Conversely, cue asynchronies initiate separate pathways and the information of the earliest cue is stored, awaiting the arrival of the later cue to control transcription. Storage mechanisms can involve changes in the activity of selected clock components or epigenetic modifications, depending on the time delay between cues (hours, days or several months). We propose a conceptual framework in which the mechanisms of integration relate to the timing of cue sensing.

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Section: Reviewmentioning

confidence: 99%

Light and temperature cues: multitasking receptors and transcriptional integrators

Casal

Qüesta

2017

New Phytologist

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“…Bacterial phytochromes can be grouped into prototypical and bathy phytochromes, in which the red-absorbing Pr and far-red-absorbing Pfr are the thermodynamically stable states, respectively 10 – 13 . The photoconversions between the parent states Pr and Pfr 14 are coupled to downstream signalling processes via the modulation of an attached output module, typically a histidine kinase 15 , 16 .…”

Section: Introductionmentioning

confidence: 99%

Structural snapshot of a bacterial phytochrome in its functional intermediate state

et al. 2018

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Phytochromes are modular photoreceptors of plants, bacteria and fungi that use light as a source of information to regulate fundamental physiological processes. Interconversion between the active and inactive states is accomplished by a photoinduced reaction sequence which couples the sensor with the output module. However, the underlying molecular mechanism is yet not fully understood due to the lack of structural data of functionally relevant intermediate states. Here we report the crystal structure of a Meta-F intermediate state of an Agp2 variant from Agrobacterium fabrum. This intermediate, the identity of which was verified by resonance Raman spectroscopy, was formed by irradiation of the parent Pfr state and displays significant reorientations of almost all amino acids surrounding the chromophore. Structural comparisons allow identifying structural motifs that might serve as conformational switch for initiating the functional secondary structure change that is linked to the (de-)activation of these photoreceptors.

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“…Since only Pr state can emit NIR fluorescence, it was evident that NIR fluorescence intensity will be enhanced. Different from other BphP-based NIR FPs, PAiRFP1 and PAiRFP2 have a PHY domain, which is essential for Pfr→Pr photoconversion [ 13 , 17 , 19 , 20 ].…”

Section: Resultsmentioning

confidence: 99%

“…When the C-terminal end of Agp2 protein is truncated, then it is called as Agrobacterium tumefaciens photosensory core domain (AtPCD). The Pr form of AtPCD protein is not stable and experiences quick dark reversion into Pfr state with a half time of 11 s [ 19 , 20 ].…”

Section: Introductionmentioning

confidence: 99%

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Comparative Analysis of Bacteriophytochrome Agp2 and Its Engineered Photoactivatable NIR Fluorescent Proteins PAiRFP1 and PAiRFP2

et al. 2020

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Two photoactivatable near infrared fluorescent proteins (NIR FPs) named “PAiRFP1” and “PAiRFP2” are formed by directed molecular evolution from Agp2, a bathy bacteriophytochrome of Agrobacterium tumefaciens C58. There are 15 and 24 amino acid substitutions in the structure of PAiRFP1 and PAiRFP2, respectively. A comprehensive molecular exploration of these bacteriophytochrome photoreceptors (BphPs) are required to understand the structure dynamics. In this study, the NIR fluorescence emission spectra for PAiRFP1 were recorded upon repeated excitation and the fluorescence intensity of PAiRFP1 tends to increase as the irradiation time was prolonged. We also predicted that mutations Q168L, V244F, and A480V in Agp2 will enhance the molecular stability and flexibility. During molecular dynamics (MD) simulations, the average root mean square deviations of Agp2, PAiRFP1, and PAiRFP2 were found to be 0.40, 0.49, and 0.48 nm, respectively. The structure of PAiRFP1 and PAiRFP2 were more deviated than Agp2 from its native conformation and the hydrophobic regions that were buried in PAiRFP1 and PAiRFP2 core exposed to solvent molecules. The eigenvalues and the trace of covariance matrix were found to be high for PAiRFP1 (597.90 nm2) and PAiRFP2 (726.74 nm2) when compared with Agp2 (535.79 nm2). It was also found that PAiRFP1 has more sharp Gibbs free energy global minima than Agp2 and PAiRFP2. This comparative analysis will help to gain deeper understanding on the structural changes during the evolution of photoactivatable NIR FPs. Further work can be carried out by combining PCR-based directed mutagenesis and spectroscopic methods to provide strategies for the rational designing of these PAiRFPs.

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Phytochromes from Agrobacterium fabrum

Cited by 25 publications

References 106 publications

Light and temperature cues: multitasking receptors and transcriptional integrators

Light and temperature cues: multitasking receptors and transcriptional integrators

Structural snapshot of a bacterial phytochrome in its functional intermediate state

Comparative Analysis of Bacteriophytochrome Agp2 and Its Engineered Photoactivatable NIR Fluorescent Proteins PAiRFP1 and PAiRFP2

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