Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria

Boulay, Clémence; Wilson, Adjélé; D’Haene, Sandrine; Kirilovsky, Diana

doi:10.1073/pnas.1002912107

Cited by 131 publications

(114 citation statements)

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“…The 1 O 2 quencher activity of the RCP was also compared with that of the fluorescence recovery protein. This protein of 14 kD, which does not bind any chromophore, is involved in the OCP-related photoprotective mechanism (Boulay et al, 2010). RCP showed the same efficiency of quenching 1 O 2 as the fluorescence recovery protein ( Figure 5C).…”

Section: Ocp Quenches 1 O 2 More Efficiently Than Red Carotenoid Protmentioning

confidence: 84%

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

et al. 2014

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Cyanobacteria have developed a photoprotective mechanism that decreases the energy arriving at the photosynthetic reaction centers under high-light conditions. The photoactive orange carotenoid protein (OCP) is essential in this mechanism as a light sensor and energy quencher. When OCP is photoactivated by strong blue-green light, it is able to dissipate excess energy as heat by interacting with phycobilisomes. As a consequence, charge separation and recombination leading to the formation of singlet oxygen diminishes. Here, we demonstrate that OCP has another essential role. We observed that OCP also protects Synechocystis cells from strong orange-red light, a condition in which OCP is not photoactivated. We first showed that this photoprotection is related to a decrease of singlet oxygen concentration due to OCP action. Then, we demonstrated that, in vitro, OCP is a very good singlet oxygen quencher. By contrast, another carotenoid protein having a high similarity with the N-terminal domain of OCP is not more efficient as a singlet oxygen quencher than a protein without carotenoid. Although OCP is a soluble protein, it is able to quench the singlet oxygen generated in the thylakoid membranes. Thus, OCP has dual and complementary photoprotective functions as an energy quencher and a singlet oxygen quencher.

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Section: Ocp Quenches 1 O 2 More Efficiently Than Red Carotenoid Protmentioning

confidence: 84%

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

et al. 2014

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“…The construction of the pCB9 plasmid, in which the frp gene (slr1964) is under control of a T7 promoter, was described in ref. 8. The point mutations were added in the short FRP gene by site-directed mutagenesis using the Quickchange XL site-directed mutagenesis kit (Stratagene) and synthetic mutagenic oligonucleotides (all of the oligonucleotides used in this work are described in Table S5).…”

Section: Methodsmentioning

confidence: 99%

“…This reversion is greatly affected by the presence of the fluorescence recovery protein (FRP) (8). In vitro, the FRP accelerates the conversion of free OCP r back to the orange form.…”

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confidence: 99%

“…In vitro, the FRP accelerates the conversion of free OCP r back to the orange form. In vivo, the FRP is essential to recover the full capacity of the antenna, presumably by playing a role in detaching OCP r from the phycobilisomes (8). Mutant strains of cyanobacteria lacking this protein are unable to recover the normal antenna capacity under low light conditions.…”

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“…The FRP from Synechocystis sp. PCC 6803 was first characterized in a form containing an additional 25 aa compared with the FRP from almost all other strains (the other exception is the FRP encoded in the Microcystis aeruginosa genome) (8). It has recently been shown that this longer form is caused by a misidentified start site, and the active form in vivo is a shorter protein that begins with Met26 (10); we have used this form for this study.…”

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Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria

Sutter

Wilson

Leverenz

et al. 2013

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

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Photosynthetic reaction centers are sensitive to high light conditions, which can cause damage because of the formation of reactive oxygen species. To prevent high-light induced damage, cyanobacteria have developed photoprotective mechanisms. One involves a photoactive carotenoid protein that decreases the transfer of excess energy to the reaction centers. This protein, the orange carotenoid protein (OCP), is present in most cyanobacterial strains; it is activated by high light conditions and able to dissipate excess energy at the site of the light-harvesting antennae, the phycobilisomes. Restoration of normal antenna capacity involves the fluorescence recovery protein (FRP). The FRP acts to dissociate the OCP from the phycobilisomes by accelerating the conversion of the active red OCP to the inactive orange form. We have determined the 3D crystal structure of the FRP at 2.5 Å resolution. Remarkably, the FRP is found in two very different conformational and oligomeric states in the same crystal. Based on amino acid conservation analysis, activity assays of FRP mutants, FRP:OCP docking simulations, and coimmunoprecipitation experiments, we conclude that the dimer is the active form. The second form, a tetramer, may be an inactive form of FRP. In addition, we have identified a surface patch of highly conserved residues and shown that those residues are essential to FRP activity. nonphotochemical quenching | Synechocystis L ight is vital for the survival and growth of photosynthetic organisms. In natural environments, these organisms are exposed to varying light conditions in addition to the day/night cycle. Too much exposure to light causes the formation of reactive oxygen species that damage the sensitive photochemical reaction centers, and thus, a careful regulation of energy flow is critical. Under low light conditions, an efficient energy collection by the antennae complexes is achieved, whereas under high light conditions, the excess energy has to be diverted from photosynthesis (1).Plants and cyanobacteria have evolved different ways to deal with excess energy arriving at the reaction centers. Higher plants and green algae contain antenna complexes consisting of transmembrane proteins that sense the acidification of the thylakoid lumen and react by switching from efficient energy collection to heat dissipation (1, 2). Cyanobacteria, however, contain antenna complexes called phycobilisomes, which are membrane-anchored and consist of phycobilin proteins. Instead of sensing the effect of high light through pH changes, cyanobacterial phycobilisomes are quenched by a protein capable of directly sensing high light conditions, the orange carotenoid protein (OCP). The 35 kDa OCP consists of two distinct domains that encompass a ketocarotenoid (3′-hydroxyechinenone) in an all trans conformation (3-6). Irradiance with high light changes the OCP from an inactive orange (OCP o ) to an active red form (OCP r ) that is capable of binding to the phycobilisomes to prevent excess energy from flowing to the reaction centers. ...

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Deletion of the short N‐terminal extension in OCP reveals the main site for FRP binding

et al. 2017

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The orange carotenoid protein (OCP) plays a key role in cyanobacterial photoprotection. Photoconversion entails structural rearrangements in OCP that are required for its binding to phycobilisome, thereby inducing excitation energy dissipation. Detachment of OCP from phycobilisome requires the fluorescence recovery protein (FRP). It is considered that OCP interacts with FRP only in the photoactivated state; however, the binding site for FRP is currently unknown. As an important stabilizing element in orange OCP, the short αA-helix within the N-terminal extension (NTE) binds to the C-terminal domain (CTD), but unfolds upon photoactivation and interferes with phycobilisome binding. Here, we demonstrate that the NTE shares specific structural and functional similarities with FRP and discover the main site of OCP-FRP interactions in the OCP-CTD.

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Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria

Cited by 131 publications

References 24 publications

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

The Cyanobacterial Photoactive Orange Carotenoid Protein Is an Excellent Singlet Oxygen Quencher

Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria

Deletion of the short N‐terminal extension in OCP reveals the main site for FRP binding

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