1H, 15N, and 13C chemical shift assignments of cyanobacteriochrome NpR6012g4 in the red-absorbing dark state

Yu, Qinhong; Lim, Sunghyuk; Rockwell, Nathan C.; Martin, Shelley S.; Lagarias, J. Clark; Ames, James B.

doi:10.1007/s12104-015-9653-8

Cited by 6 publications

(5 citation statements)

References 12 publications

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“…This spectrum closely resembles the one of the SPH model that we have found to be exclusively in the D-αf conformation. This finding is in line with recent NMR studies on NpR6012g4 that assign the histidine 688 (analog of H322 in AnPixJg2) to be neutral and the structure of the chromophore to be homogeneous in the ground state in agreement with our SPH model (7,14).…”

Section: Tryptophan (W289) Dynamicssupporting

confidence: 92%

Histidine protonation controls structural heterogeneity in the cyanobacteriochrome AnPixJg2

Rao

Wiebeler

Sen

et al. 2021

Phys. Chem. Chem. Phys.

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Section: Tryptophan (W289) Dynamicssupporting

confidence: 92%

Histidine protonation controls structural heterogeneity in the cyanobacteriochrome AnPixJg2

Rao

Wiebeler

Sen

et al. 2021

Phys. Chem. Chem. Phys.

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“…AnPixJg2 is closely related to NpR6012g4 from Nostoc punctiforme (35), which has been shown to be photochemically heterogeneous on the ultrafast timescale (36)(37)(38)(39). NpR6012g4 has also been characterized using solution NMR, with complete chromophore chemical shift assignments and secondary structure already reported for both photostates (40)(41)(42)(43).…”

Section: Significancementioning

confidence: 98%

“…We previously reported secondary-structure assignments (Biological Magnetic Resonance Bank accession numbers 26577 and 26582) and chromophore chemical shifts for NpR6012g4 in both photostates (40)(41)(42)(43). We used these assignments to derive structural restraints and perform high-resolution structural analysis of both photostates.…”

Section: Determination Of Solution Structures For Both Photostates Ofmentioning

confidence: 99%

Correlating structural and photochemical heterogeneity in cyanobacteriochrome NpR6012g4

Lim

Gottlieb

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

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139

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Phytochrome photoreceptors control plant growth, development, and the shade avoidance response that limits crop yield in high-density agricultural plantings. Cyanobacteriochromes (CBCRs) are distantly related photosensory proteins that control cyanobacterial metabolism and behavior in response to light. Photoreceptors in both families reversibly photoconvert between two photostates via photoisomerization of linear tetrapyrrole (bilin) chromophores. Spectroscopic and biochemical studies have demonstrated heterogeneity in both photostates, but the structural basis for such heterogeneity remains unclear. We report solution NMR structures for both photostates of the red/green CBCR NpR6012g4 from In addition to identifying structural changes accompanying photoconversion, these structures reveal structural heterogeneity for residues Trp655 and Asp657 in the red-absorbing NpR6012g4 dark state, yielding two distinct environments for the phycocyanobilin chromophore. We use site-directed mutagenesis and fluorescence and absorbance spectroscopy to assign an orange-absorbing population in the NpR6012g4 dark state to the minority configuration for Asp657. This population does not undergo full, productive photoconversion, as shown by time-resolved spectroscopy and absorption spectroscopy at cryogenic temperature. Our studies thus elucidate the spectral and photochemical consequencesof structural heterogeneity in a member of the phytochrome superfamily, insights that should inform efforts to improve photochemical or fluorescence quantum yields in the phytochrome superfamily.

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“…Typically, the Phys reversibly respond to red and far‐red light, whereas the CBCRs sense an extremely wide wavelength range from ultraviolet to far‐red light . Among them, PCB‐binding red/green‐type CBCR GAF domains that reversibly photoconvert between the red light‐absorbing form with 15 Z ‐isomer (Pr) and the green light‐absorbing form with 15 E ‐isomer (Pg) are found widely in various cyanobacteria and have been extensively characterized using various spectroscopic techniques .…”

Section: Introductionmentioning

confidence: 99%

Distinctive Properties of Dark Reversion Kinetics between Two Red/Green‐Type Cyanobacteriochromes and their Application in the Photoregulation of cAMP Synthesis

Fushimi

Enomoto

Ikeuchi

et al. 2017

Photochem & Photobiology

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Cyanobacteriochromes (CBCRs) are photoreceptors that bind to a linear tetrapyrrole within a conserved cGMP-phosphodiesterase/adenylate cyclase/FhlA (GAF) domain and exhibit reversible photoconversion. Red/green-type CBCR GAF domains that photoconvert between red- (Pr) and green-absorbing (Pg) forms occur widely in various cyanobacteria. A putative phototaxis regulator, AnPixJ, contains multiple red/green-type CBCR GAF domains. We previously reported that AnPixJ's second domain (AnPixJg2) but not its fourth domain (AnPixJg4) shows red/green reversible photoconversion. Herein, we found that AnPixJg4 showed Pr-to-Pg photoconversion and rapid Pg-to-Pr dark reversion, whereas AnPixJg2 showed a barely detectable dark reversion. Site-directed mutagenesis revealed the involvement of six residues in Pg stability. Replacement at the Leu294/Ile660 positions of AnPixJg2/AnPixJg4 showed the highest influence on dark reversion kinetics. AnPixJg2_DR6, wherein the six residues of AnPixJg2 were entirely replaced with those of AnPixJg4, showed a 300-fold faster dark reversion than that of the wild type. We constructed chimeric proteins by fusing the GAF domains with adenylate cyclase catalytic regions, such as AnPixJg2-AC, AnPixJg4-AC and AnPixJg2_DR6-AC. We detected successful enzymatic activation under red light for both AnPixJg2-AC and AnPixJg2_DR6-AC, and repression under green light for AnPixJg2-AC and under dark incubation for AnPixJg2_DR6-AC. These results provide platforms to develop cAMP synthetic optogenetic tools.

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1H, 15N, and 13C chemical shift assignments of cyanobacteriochrome NpR6012g4 in the red-absorbing dark state

Cited by 6 publications

References 12 publications

Histidine protonation controls structural heterogeneity in the cyanobacteriochrome AnPixJg2

Histidine protonation controls structural heterogeneity in the cyanobacteriochrome AnPixJg2

Correlating structural and photochemical heterogeneity in cyanobacteriochrome NpR6012g4

Distinctive Properties of Dark Reversion Kinetics between Two Red/Green‐Type Cyanobacteriochromes and their Application in the Photoregulation of cAMP Synthesis

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