A Truncated Mutant of the Extrinsic 23-kDa Protein that Absolutely Requires the Extrinsic 17-kDa Protein for Ca2+ Retention in Photosystem II

Ifuku, Kentaro; Sato, Fumihiko

doi:10.1093/pcp/pcf136

Cited by 38 publications

(30 citation statements)

References 27 publications

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“…2 A and B). Our identification of interacting domains between PsbP and PsbQ helps explain the observation that PsbQ assists in the stabilization of PsbP binding and function (32,33). This observation may also explain why loop 3A is disordered and not resolved in the current PsbP crystal structure.…”

Section: Resultsmentioning

confidence: 52%

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Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

Mummadisetti

Frankel

Bellamy

et al. 2014

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

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Protein cross-linking and radiolytic footprinting coupled with highresolution mass spectrometry were used to examine the structure of PsbP and PsbQ when they are bound to Photosystem II. In its bound state, the N-terminal 15-amino-acid residue domain of PsbP, which is unresolved in current crystal structures, interacts with domains in the C terminus of the protein. These interactions may serve to stabilize the structure of the N terminus and may facilitate PsbP binding and function. These interactions place strong structural constraints on the organization of PsbP when associated with the Photosystem II complex. Additionally, amino acid residues in the structurally unresolved loop 3A domain of PsbP ( 90 K-107 V), 93 Y and 96 K, are in close proximity (≤11.4 Å) to the N-terminal 1 E residue of PsbQ. These findings are the first, to our knowledge, to identify a putative region of interaction between these two components. Cross-linked domains within PsbQ were also identified, indicating that two PsbQ molecules can interact in higher plants in a manner similar to that observed by Liu et al. [(2014) Proc Natl Acad Sci 111 (12):4638-4643] in cyanobacterial Photosystem II. This interaction is consistent with either intra-Photosystem II dimer or inter-Photosystem II dimer models in higher plants. Finally, OH • produced by synchrotron radiolysis of water was used to oxidatively modify surface residues on PsbP and PsbQ. Domains on the surface of both protein subunits were resistant to modification, indicating that they were shielded from water and appear to define buried regions that are in contact with other Photosystem II components.oxidoreductase that is found in all oxygenic photosynthetic organisms. This membrane protein complex contains at least 20 protein subunits, 17 of which are intrinsic membrane proteins. Higher plants contain three extrinsic proteins associated with the complex-PsbO, PsbP, and PsbQ-whereas cyanobacteria contain PsbO, PsbU, PsbV, and CyanoQ (a homolog of PsbQ). In higher plants the PsbO, PsbP, and PsbQ proteins are required for optimal rates of O 2 evolution under physiological inorganic calcium and chloride concentrations (1, 2).The PsbO protein appears to play a central role in the stabilization of the manganese cluster in all oxygenic photosynthetic organisms (3). In higher plants, PsbO and PsbP are required for photoautotrophic growth, PS II assembly, and the stabilization of PS II supercomplexes (4-9), with PsbP also being required for normal thylakoid assembly (6). Under low-light growth conditions, PsbQ is required for photoautotrophy (10).Although the crystal structure of cyanobacterial PS II has been resolved to 1.9 Å (11), no crystal structures for higher plant PS II have been presented. The structure and interactions of PsbO with the intrinsic subunits have been approximated by analogy to the cyanobacterial photosystem. Although high-resolution crystal structures of isolated spinach PsbP [1.98 Å; Protein Data Bank (PDB) ID code 2VU4] (12) and PsbQ (1.49 Å; PDB ID code 1VYK) are avai...

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Section: Resultsmentioning

confidence: 52%

“…An N-terminal 19-amino-acid residue-truncated PsbP cannot bind to PS II in the absence of PsbQ but can bind in its presence. Importantly, in the presence of PsbQ, the function of the truncated PsbP is partially restored (32,33).…”

Section: Resultsmentioning

confidence: 99%

Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

Mummadisetti

Frankel

Bellamy

et al. 2014

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

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“…The activity of isolated PSII membranes was ϳ480 mol O 2 /mg Chl/h. The reconstitution of PsbP to NaCl-washed PSII membranes and the measurement of O 2 evolution were performed according to a procedure reported elsewhere (27,30) with a slight modification: To stabilize the interaction of the extrinsic proteins and the NaCl-washed PSII membranes, 0.4 M sucrose was replaced with 2 M betaine in the reconstitution buffer (25 mM Mes-NaOH, pH 6.5, 2 M betaine, 20 mM CaCl 2 ) and in the activity measurement buffer (25 mM Mes-NaOH, pH 6.5, 2 M betaine). PsbP was reconstituted with PSII in molecular ratio of 2:1 (PsbP:PSII), unless otherwise noted.…”

Section: Methodsmentioning

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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“…In this study, we re-investigated the role of N-terminal region of PsbP on the basis of its three-dimensional structure. In previous paper [Ifuku and Sato (2002) Plant Cell Physiol 43: 1244-1249], a truncated PsbP lacking 19 N-terminal residues (D19) was found to bind to NaCl-washed PS II lacking PsbP and PsbQ without activation of oxygen evolution at all. Three-dimensional (3D) structure of PsbP suggests that deletion of 19 N-terminal residues would destabilize its protein structure, as indicated by the high sensitivity of D19 to trypsin digestion.…”

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confidence: 99%

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

et al. 2005

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PsbP is a membrane extrinsic subunit of Photosystem II (PS II), which is involved in retaining Ca2+ and Cl-, two inorganic cofactors for the water-splitting reaction. In this study, we re-investigated the role of N-terminal region of PsbP on the basis of its three-dimensional structure. In previous paper [Ifuku and Sato (2002) Plant Cell Physiol 43: 1244-1249], a truncated PsbP lacking 19 N-terminal residues (Delta19) was found to bind to NaCl-washed PS II lacking PsbP and PsbQ without activation of oxygen evolution at all. Three-dimensional (3D) structure of PsbP suggests that deletion of 19 N-terminal residues would destabilize its protein structure, as indicated by the high sensitivity of Delta19 to trypsin digestion. Thus, a truncated PsbP lacking 15 N-terminal residues (Delta15), which retained core PsbP structure, was produced. Whereas Delta15 was resistant to trypsin digestion and bound to NaCl-washed PS II membranes, it did not show the activation of oxygen evolution. This result indicated that the interaction of 15-residue N-terminal flexible region of PsbP with PS II was important for Ca2+ and Cl- retention in PS II, although the 15 N-terminal residues were not essential for the binding of PsbP to PS II. The possible N-terminal residues of PsbP that would be involved in this interaction are discussed.

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A Truncated Mutant of the Extrinsic 23-kDa Protein that Absolutely Requires the Extrinsic 17-kDa Protein for Ca2+ Retention in Photosystem II

Cited by 38 publications

References 27 publications

Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant 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

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

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