Cyanobacteriochrome CcaS regulates phycoerythrin accumulation in
            <i>Nostoc punctiforme</i>
            , a group II chromatic adapter

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

doi:10.1073/pnas.1000177107

Cited by 121 publications

(144 citation statements)

References 41 publications

(45 reference statements)

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“…1C), indicative of the α-facial bilin D-ring in both 15Z and 15E states (25,42) seen in many CBCRs (19,23,24). These features of RcaE are very similar to those previously described for CcaS (16,40), implicating a conserved green/red photocycle in known CCA photoreceptors.…”

Section: Resultssupporting

confidence: 67%

“…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%

“…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). CcaS functions in a two-component phosphorelay pathway to regulate CCA in N. punctiforme (40), with phycoerythrin being regulated (type II CCA) (36).…”

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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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Section: Resultssupporting

confidence: 67%

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confidence: 99%

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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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142

265

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“…The recently identified cyanobacteriochromes (CBCRs) mediate photochromatic and phototactic responses in cyanobacteria (1)(2)(3). Great strides toward a molecular understanding of photoreception and signal transduction in this spectrally diverse and exciting photoreceptor family have now been taken by Narikawa et al (4), who report highresolution structures of two CBCR photosensor modules in PNAS.…”

mentioning

confidence: 99%

“…Multiple CBCRs often occur in tandem within a single protein, allowing integration of multiple light signals at a single C-terminal output domain (10). Whereas Phys predominantly respond to the red/far-red spectral region, CBCRs display a rich variety of photocycles spanning the entire visible and near-UV spectrum (2,(11)(12)(13). At least four subfamilies of CBCRs can be distinguished on the basis of their underlying photochemistry and primary structure.…”

mentioning

confidence: 99%