Cyanobacteriochrome CcaS is the green light receptor that induces the expression of phycobilisome linker protein

Hirose, Yuu; Shimada, Takashi; Narikawa, Rei; Katayama, Mikio; Ikeuchi, Masahiko

doi:10.1073/pnas.0801826105

Cited by 228 publications

(294 citation statements)

References 35 publications

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“…S1C) (19,25). Such a second Cys is not found in CBCR subfamilies sensing green to red light (520-670 nm) (16,17), implicating other mechanisms allowing perception of green light by the intrinsically red-absorbing bilin chromophore.…”

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confidence: 99%

“…* Cyanobacteriochromes (CBCRs) are widespread cyanobacterial photosensors with phytochrome-related GAF domains (1,2,13,14). Although CBCRs also convert between two photostates via bilin photoisomerization at C15, they exhibit much more spectral diversity, with peak absorptions ranging from 330 to 680 nm and hence spanning the entire visible spectrum and near UV (13,(15)(16)(17)(18)(19)(20)(21)(22)(23)(24). CBCR subfamilies that sense light in the near-UV to blue region (330-470 nm) have been studied extensively.…”

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confidence: 99%

“…Homologous CcaS CBCRs from Synechocystis sp. PCC 6803 and Nostoc punctiforme ATCC 29133 recently were characterized (16,40). CcaS proteins contain a CBCR GAF domain closely related to that of RcaE, photoconvert between a green-absorbing dark state ( 15Z P g ) and a redabsorbing photoproduct ( 15E P r ), and exhibit green-stimulated histidine kinase activity (16).…”

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confidence: 99%

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Green/red cyanobacteriochromes regulate complementary chromatic acclimation via a protochromic photocycle

Hirose

Rockwell

Nishiyama

et al. 2013

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

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Cyanobacteriochromes (CBCRs) are cyanobacterial members of the phytochrome superfamily of photosensors. Like phytochromes, CBCRs convert between two photostates by photoisomerization of a covalently bound linear tetrapyrrole (bilin) chromophore. Although phytochromes are red/far-red sensors, CBCRs exhibit diverse photocycles spanning the visible spectrum and the near-UV (330-680 nm). Two CBCR subfamilies detect near-UV to blue light (330-450 nm) via a "two-Cys photocycle" that couples bilin 15Z/15E photoisomerization with formation or elimination of a second bilincysteine adduct. On the other hand, mechanisms for tuning the absorption between the green and red regions of the spectrum have not been elucidated as of yet. CcaS and RcaE are members of a CBCR subfamily that regulates complementary chromatic acclimation, in which cyanobacteria optimize light-harvesting antennae in response to green or red ambient light. CcaS has been shown to undergo a green/red photocycle: reversible photoconversion between a green-absorbing 15Z state ( 15Z P g ) and a red-absorbing 15E state ( 15E P r ). We demonstrate that RcaE from Fremyella diplosiphon undergoes the same photocycle and exhibits light-regulated kinase activity. In both RcaE and CcaS, the bilin chromophore is deprotonated as 15Z P g but protonated as 15E P r . This change of bilin protonation state is modulated by three key residues that are conserved in green/red CBCRs. We therefore designate the photocycle of green/red CBCRs a "protochromic photocycle," in which the dramatic change from green to red absorption is not induced by initial bilin photoisomerization but by a subsequent change in bilin protonation state.light sensing | phycobiliprotein | signal transduction | spectral tuning | two-component signaling P hytochrome photosensors initially were discovered in plants and later found in cyanobacteria, nonoxygenic photosynthetic bacteria, nonphotosynthetic bacteria, fungi, and algae (1, 2). These photoreceptors bind linear tetrapyrrole (bilin) chromophores within a conserved GAF (cGMP phosphodiesterase/adenylyl cyclase/FhlA) domain via a covalent thioether linkage to a conserved Cys residue (Fig. S1A)(3-6). Upon illumination, phytochromes reversibly convert between a red-absorbing dark state and a far-red-absorbing photoproduct. This red/far-red photocycle is triggered by photoisomerization of the bilin 15,16-double bond between the 15Z and 15E configurations (7,8), with 15Z giving red absorption and 15E far-red absorption (4, 6, 9). In phytochromes, the conjugated π system of the bilin is protonated in both photostates, and this protonation is necessary to maintain the red and far-red absorption (10-12). Conserved GAF residues supply a hydrogen bond network to tune the chemical and spectral properties of the bilin (Fig. S1B).* Cyanobacteriochromes (CBCRs) are widespread cyanobacterial photosensors with phytochrome-related GAF domains (1,2,13,14). Although CBCRs also convert between two photostates via bilin photoisomerization at C15, they exhibit much more spe...

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Green/red cyanobacteriochromes regulate complementary chromatic acclimation via a protochromic photocycle

Hirose

Rockwell

Nishiyama

et al. 2013

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

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142

265

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“…Pt-DPH-FL and Tp-DPH-PSM dark relaxation was followed during 24 h at room temperature starting from DPH purified under room lighting. Autophosphorylation assay was performed with ;16.8 µM Pt-DPH-FL holoprotein as described (Hirose et al, 2008), under irradiation with R or FR light up to 3 min.…”

Section: Expression Purification and Spectral Analysis Of Dph Proteinsmentioning

confidence: 99%

Diatom Phytochromes Reveal the Existence of Far-Red-Light-Based Sensing in the Ocean

et al. 2016

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The absorption of visible light in aquatic environments has led to the common assumption that aquatic organisms sense and adapt to penetrative blue/green light wavelengths but show little or no response to the more attenuated red/far-red wavelengths. Here, we show that two marine diatom species, Phaeodactylum tricornutum and Thalassiosira pseudonana, possess a bona fide red/far-red light sensing phytochrome (DPH) that uses biliverdin as a chromophore and displays accentuated red-shifted absorbance peaks compared with other characterized plant and algal phytochromes. Exposure to both red and far-red light causes changes in gene expression in P. tricornutum, and the responses to far-red light disappear in DPH knockout cells, demonstrating that P. tricornutum DPH mediates far-red light signaling. The identification of DPH genes in diverse diatom species widely distributed along the water column further emphasizes the ecological significance of far-red light sensing, raising questions about the sources of far-red light. Our analyses indicate that, although far-red wavelengths from sunlight are only detectable at the ocean surface, chlorophyll fluorescence and Raman scattering can generate red/far-red photons in deeper layers. This study opens up novel perspectives on phytochrome-mediated far-red light signaling in the ocean and on the light sensing and adaptive capabilities of marine phototrophs.

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“…PixJ1 has an ability for photoreversible conversion between a BL absorbing form, P b (λ max =425-435 nm), and a GL absorbing form, P g (λ max =535 nm; Yoshihara et al 2004). Another cyanobacteriochrome, CcaS, also exhibits photoreversible conversion between GL and RL (Hirose et al 2008). However, these photoreceptors are only found in Cyanobacteria, not in stramenopile algae.…”

Section: Correlation Between Morphology and Motilitymentioning

confidence: 99%

Analysis of Light-Dependent Cell Morphology and an Accumulation Response in <i>Ochromonas danica</i>

2012

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Summary Recently, we discovered the LOV-containing blue light (BL) receptor, aureochrome, in the stramenopile alga Vaucheria. Aureochrome has been isolated in other stramenopile algae, such as Fucus and Ochromonas. The functional role of aureochrome has still not been identified in Fucus and Ochromonas. What kind of response does aureochrome mediate? Here, we investigated various light responses, such as cell morphology, motility and behavior in Ochromonas danica, by measuring cell dimensions and observing swimming behavior under various light conditions. Although cell length was not changed by different wavelengths of light (BL, GL and RL), cell width decreased in BL and GL in comparison with RL; that is RL-cultured cells are more spherical relative to those cultured in BL or GL. Also, the swimming speed of O. danica is slower under RL than under BL or GL. There was also an accumulation response toward a small irradiated area, but this response was induced only by BL or GL, not RL. The possible involvement of photoreceptors absorbing BL and GL in these morphological and motility responses is discussed.

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Cyanobacteriochrome CcaS is the green light receptor that induces the expression of phycobilisome linker protein

Cited by 228 publications

References 35 publications

Green/red cyanobacteriochromes regulate complementary chromatic acclimation via a protochromic photocycle

Green/red cyanobacteriochromes regulate complementary chromatic acclimation via a protochromic photocycle

Diatom Phytochromes Reveal the Existence of Far-Red-Light-Based Sensing in the Ocean

Analysis of Light-Dependent Cell Morphology and an Accumulation Response in <i>Ochromonas danica</i>

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