Partial degradation of the extrinsic 23-kDa protein of the Photosystem II complex of spinach

Miyao, Mitsue; Fujimura, Yoko; Murata, Norio

doi:10.1016/0005-2728(88)90024-2

Cited by 38 publications

(25 citation statements)

References 22 publications

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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%

“…Furthermore, the interaction site between PsbP and PSII has been identified as the Ala-1 on PsbP and the Glu-57 of PsbE. Previous reports have suggested that the truncation of the first nine N-terminal residues specifically impairs the ability of PsbP to retain Cl Ϫ (38). This suggests that the C-terminal domain of PsbP, including the local structure around His-144 and Asp-165, has a role of binding its N-terminal sequence to exactly the right position in PSII inducing proper conformation around the Cl Ϫ binding site.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

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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“…At 0 mM BS3, both PsbP and PsbQ appeared to exhibit proteolysis in the NaCl-wash extracts. It had been shown previously that both of these proteins are susceptible to proteolytic attack (17)(18)(19). The presence of the cross-linker BS3, however, appeared to suppress this endogenous proteolytic activity.…”

Section: Resultsmentioning

confidence: 80%

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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“…Since there is no structural information available for the extrinsic subunits of PSII, it was necessary to take a systematic approach to the mutational analysis of the OE23 polypeptide. Although very little data exist concerning the binding properties of specific OE23 protein domains, reconstitution studies of native and protease-treated OE23 have suggested that the amino-terminal portion of the mature protein is not essential for functional binding to the PSII complex (Miyao et al, 1988). Using this information we initially generated a series of truncations from the carboxyl end of the polypeptide utilizing existing unique restriction sites in the cDNA.…”

Section: Modifications Of the O E 2 3 Precursormentioning

confidence: 99%

“…Depletion and reconstitution experiments using detergent-isolated PSII membranes or inside-out thylakoids have provided some information about how the OEC subunits are assembled (reviewed by Ghanotakis and Yocum, 1990). Rebinding experiments have shown that the presence of the OE33 subunit facilitates the binding of the OE23 protein, although OE23 associates with the complex in the absence of bound OE33 (Miyao et al, 1988;Miyao and Murata, 1989). The binding of OE33 to the integral PSII components appears to result in a conformational change in the complex that may either enhance an intrinsic OE23-binding site or create a binding site on OE33 itself (Miyao and Murata, 1989).…”

mentioning

confidence: 99%

Analysis of the Import of Carboxyl-Terminal Truncations of the 23-Kilodalton Subunit of the Oxygen-Evolving Complex Suggests That Its Structure Is an Important Determinant for Thylakoid Transport

Roffey

Theg

1996

Plant Physiology

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A series of deletions from the carboxyl terminus of the 23-kD subunit of the photosynthetic oxygen-evolving complex OE23 revealed that these truncations result i n various degrees of inhibition of translocation across thylakoid membranes and their subsequent assembly to the oxygen-evolving complex. lmport of in vitro translated precursors across the chloroplast envelopes was not inhibited by these truncations. Time-course studies of the import of truncated OE23 precursors into intact chloroplasts revealed that the stromal intermediate was subsequently translocated into the thylakoid lumen, where it was processed to a smaller size and rapidly degraded.I n contrast to the full-length OE23 intermediate, the truncated intermediate forms that accumulated in the stroma as a result of de-energization of thylakoid membranes could be found associated with the membrane rather than free in the stroma. Protease digestion experiments revealed that the deletions evidently altered the folded conformation of the protein. These results suggest that the carboxyl-terminal portion of the OE23 precursor is important for the maintenance of an optimal structure for import into thylakoids, implying that the efficient translocation of OE23 requires the protein to be correctly folded. In addition, the rapid degradation of the truncated forms of the processed OE23 within the lumen indicates that a protease (or proteases) active in the lumen can recognize and remove misfolded polypeptides.Within the chloroplast, the multisubunit PSII protein complex is the site of catalysis for the conversion of water to molecular oxygen as a result of photosynthetic electron transfer across thylakoid membranes. The minimal PSII preparation from eukaryotic photosynthetic membranes that is able to catalyze oxygen evolution consists of the 32-and 34-kD integral protein subunits known as D1 and D2, which make up the core of the reaction center; the a and p subunits of Cyt b559; the core antenna components CP43 and CP47; and severa1 other small polypeptides (reviewed by Debus, 1992;Vermaas, 1993). Most oxygen-evolving preparations also contain a 33-kD extrinsic protein (OE33), although its presence is not strictly required for this activity. Two additional extrinsic protein components of 23 and 17 kD (OE23 and OE17) also are associated with a more intact oxygen-evolving membrane preparation. The extrinsic subunits of the OEC, OE33,OE23, and OE17 are tightly bound to the lumen-exposed domains of the PSII complex. Loss of the OE23 and OE17 proteins has been correlated with lowered rates of oxygen evolution, but because depleted membranes retain the ability to catalyze water oxidation, these polypeptides are considered to have structural and regulatory roles, as opposed to catalytic functions, in oxygen evolution (Vermaas, 1993).The assembly of the OEC is of interest not only for its implications in mechanistic and regulatory aspects of oxygen evolution, but also because the multimeric PSII-OEC is formed with subunits encoded by both chloroplast and nuclear genes...

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Partial degradation of the extrinsic 23-kDa protein of the Photosystem II complex of spinach

Cited by 38 publications

References 22 publications

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

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

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

Analysis of the Import of Carboxyl-Terminal Truncations of the 23-Kilodalton Subunit of the Oxygen-Evolving Complex Suggests That Its Structure Is an Important Determinant for Thylakoid Transport

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