Structure and function of the PsbP protein of Photosystem II from higher plants

Ifuku, Kentaro; Nakatsu, Toru; Shimamoto, Ren; Yamamoto, Yumiko; Ishihara, Seiko; Kato, Hiroaki; Sato, Fumihiko

doi:10.1007/s11120-004-7160-3

Cited by 31 publications

(21 citation statements)

References 17 publications

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“…This result correlates well with the previous observation that reconstitution with Δ15-PsbP did not restore the PsbP function of Ca 2+ and Clretention (37). Thus, the conformational changes of the OEC induced by the interaction of the N-terminal region of PsbP likely alter the binding properties of Ca 2+ and Cl -to prevent their dissociation.…”

Section: Discussionsupporting

confidence: 91%

FTIR Evidence That the PsbP Extrinsic Protein Induces Protein Conformational Changes around the Oxygen-Evolving Mn Cluster in Photosystem II

et al. 2009

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Extrinsic proteins of photosystem II (PSII) regulate the oxygen-evolving reaction performed at the Mn cluster by controlling the binding properties of the indispensable cofactors Ca(2+) and Cl(-). However, the molecular mechanism underlying this regulation is not yet understood. We have investigated the structural couplings of the extrinsic proteins PsbO, PsbP, and PsbQ of higher plants with the Mn cluster using Fourier transform infrared (FTIR) spectroscopy. Light-induced FTIR difference spectra upon the S(1) --> S(2) transition were measured using spinach PSII membranes, and the effects of the selective depletion of extrinsic proteins were examined. Depletion of the PsbP and PsbQ proteins by NaCl washing revealed clear changes in the amide I bands with no appreciable changes in the bands of carboxylate and imidazole groups, whereas the depletion of all three proteins by CaCl(2) washing did not cause further changes. The original amide I features were recovered by reconstitution of the NaCl-washed PSII with PsbP, and the same recovery was observed with (13)C-labeled PsbP. These results indicate that the PsbP protein, but not PsbQ and PsbO, affects the protein conformation around the Mn cluster in the intrinsic proteins without changing the ligand structure. Reconstitution with Delta15-PabP, in which the 15 N-terminal residues were truncated, did not restore the amide I bands, indicating that the interaction of the N-terminal region induces the conformational changes. This observation correlates well with a previous finding that Delta15-PabP did not restore the Ca(2+) and Cl(-) retention ability upon rebinding to PSII [Ifuku, K., et al. (2005) Photosynth. Res. 84, 251-255]. Therefore, the evidence strongly suggests that protein conformational changes around the Mn cluster induced by PsbP through its N-terminal region affect the binding properties of Ca(2+) and Cl(-) and enhance their retention.

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Section: Discussionsupporting

confidence: 91%

FTIR Evidence That the PsbP Extrinsic Protein Induces Protein Conformational Changes around the Oxygen-Evolving Mn Cluster in Photosystem II

et al. 2009

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“…However, several reports suggest that PsbO can be extracted without affecting PsbP and PsbQ binding (41)(42)(43), indicating direct association of PsbP (and PsbQ) with the PSII intrinsic subunits. The direct interaction between the PsbP N terminus and PsbE is in accordance with the previous reports, showing that N-terminal residues of PsbP are important for the binding of the protein to PSII (21,38). The interaction between PsbP and PsbE was also reported in Chlamydomonas, although cross-linked residues have not been determined (44).…”

Section: Discussionsupporting

confidence: 91%

“…The locations and binding topologies of PsbP and PsbQ in the green plant PSII complex have been proposed (17,18) (19,20). Truncation of the PsbP N terminus by 15 residues resulted in a loss of the protein Ca 2ϩ and Cl Ϫ retention ability (21). In addition, we have recently reported that His-144, a highly conserved residue in PsbP and CyanoP, was important for the ion retention ability (20).…”

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confidence: 99%

The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b559 Subunit of Photosystem II

Ido

Kakiuchi

Uno

et al. 2012

Journal of Biological Chemistry

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Background:PsbP is an extrinsic subunit of photosystem II in green plants. Results: H144A mutation in PsbP alters the chloride requirement and affects the interaction between its N terminus and the PsbE component of photosystem II. Conclusion:The N-and C-terminal domains of PsbP cooperate to support PSII activity. Significance: This provides important information about the binding characteristics of PsbP in green plant PSII.The PsbP protein regulates the binding properties of Ca 2؉ and Cl ؊ , and stabilizes the Mn cluster of photosystem II (PSII); however, the binding site and topology in PSII have yet to be clarified. Here we report that the structure around His-144 and Asp-165 in PsbP, which is suggested to be a metal binding site, has a crucial role for the functional interaction between PsbP and PSII. The mutated PsbP-H144A protein exhibits reduced ability to retain Cl ؊ anions in PSII, whereas the D165V mutation does not affect PsbP function. Interestingly, H144A/D165V double mutation suppresses the effect of H144A mutation, suggesting that these residues have a role other than metal binding. FTIR difference spectroscopy suggests that H144A/D165V restores proper interaction with PSII and induces the conformational change around the Mn cluster during the S 1 /S 2 transition. Cross-linking experiments show that the H144A mutation affects the direct interaction between PsbP and the Cyt b 559 ␣ subunit of PSII (the PsbE protein). However, this interaction is restored in the H144A/D165V mutant. In the PsbP structure, His-144 and Asp-165 form a salt bridge. H144A mutation is likely to disrupt this bridge and liberate Asp-165, inhibiting the proper PsbP-PSII interaction. Finally, mass spectrometric analysis has identified the cross-linked sites of PsbP and PsbE as Ala-1 and Glu-57, respectively. Therefore His-144, in the C-terminal domain of PsbP, plays a crucial role in maintaining proper N terminus interaction. These data provide important information about the binding characteristics of PsbP in green plant PSII.Photosystem II (PSII) 2 consists of both membrane-intrinsic and membrane-extrinsic subunits, and functions as a water/ plastoquinone oxidoreductase (for reviews, Refs. 1-4). On the thylakoid lumenal side of PSII, a metal cluster of four Mn ions, one Ca 2ϩ ion, and five oxo ligands (the Mn cluster) catalyzes the oxygen-evolving reaction. Additionally, two Cl Ϫ ions are bound near to the Mn cluster (5). The membrane-intrinsic subunits of PSII are involved in pigment and/or cofactor binding for photochemical reactions, while the membrane-extrinsic subunits surround the catalytic Mn cluster and play crucial roles in stabilizing the Mn cluster and retaining the PSII cofactor ions (6 -8).X-ray structural analysis of the cyanobacterial PSII complex at atomic resolution has revealed the location of subunits, pigments, and cofactors, including the exact organization of the subunits within PSII (5, 9 -11). However, the crystallographic information gained from the study of cyanobacterial PSII cannot necessarily be...

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“…59) The N-terminal sequence of PsbP, which is not visible in the crystal structure (1.6 Å: PDB ID 1V2B 14) ), has a critical role in the specific and functional interaction of PsbP with PSII. 60,61) Given PsbQ can restore the ability of the N-terminal truncated form of PsbP to induce the proper conformational changes and activate oxygen evolution in the OEC, PsbQ is inferred to have an auxiliary role to support PsbP binding and function in higher plants. 60,62) It should be noted that PsbQ in green algae would have a different function when compared to this protein in higher plants, as the primary sequence of green-algal PsbQ is more closely related to PsbQ′ in red algae and diatoms and can be categorized to PsbQ′ (Fig.…”

Section: Additional Extrinsic Proteins: Cyanop and Cyanoqmentioning

confidence: 99%

Localization and functional characterization of the extrinsic subunits of photosystem II: an update

Ifuku

2015

Bioscience, Biotechnology, and Biochemistry

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Photosystem II (PSII), which catalyzes photosynthetic water oxidation, is composed of more than 20 subunits, including membrane-intrinsic and -extrinsic proteins. The extrinsic proteins of PSII shield the catalytic Mn4CaO5 cluster from exogenous reductants and serve to optimize oxygen evolution at physiological ionic conditions. These proteins include PsbO, found in all oxygenic organisms, PsbP and PsbQ, specific to higher plants and green algae, and PsbU, PsbV, CyanoQ, and CyanoP in cyanobacteria. Furthermore, red algal PSII has PsbQ' in addition to PsbO, PsbV, and PsbU, and diatoms have Psb31 in supplement to red algal-type extrinsic proteins, exemplifying the functional divergence of these proteins during evolution. This review provides an updated summary of recent findings on PSII extrinsic proteins and discusses their binding, function, and evolution within various photosynthetic organisms.

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Structure and function of the PsbP protein of Photosystem II from higher plants

Cited by 31 publications

References 17 publications

FTIR Evidence That the PsbP Extrinsic Protein Induces Protein Conformational Changes around the Oxygen-Evolving Mn Cluster in Photosystem II

FTIR Evidence That the PsbP Extrinsic Protein Induces Protein Conformational Changes around the Oxygen-Evolving Mn Cluster in Photosystem II

The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b559 Subunit of Photosystem II

Localization and functional characterization of the extrinsic subunits of photosystem II: an update

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