Structure of Psb27 in Solution: Implications for Transient Binding to Photosystem II during Biogenesis and Repair

Cormann, Kai U.; Bangert, Jan-Amadé; Ikeuchi, Masahiko; Rögner, Matthias; Stoll, Raphael; Nowaczyk, Marc M.

doi:10.1021/bi9012726

Cited by 43 publications

(34 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This orientation takes into account any serious structural conflicts between Psb27 and loop A of the D1 protein. A spatial conflict, however, may still occur between the H2-H3 loop of Psb27 (9) and the N-terminal 10 aa residues of PsbO (PDB ID 3ARC). An implication of such a spatial conflict is that the binding affinity of PsbO is reduced significantly in the presence of Psb27 in the PSII assembly intermediates, consistent with the experimental observation that PsbO is absent in all ΔctpA PSII preparations (6, 11).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates

Liu¹,

Huang

Chen

et al. 2011

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

View full text Add to dashboard Cite

Photosystem II (PSII), a large multisubunit pigment-protein complex localized in the thylakoid membrane of cyanobacteria and chloroplasts, mediates light-driven evolution of oxygen from water. Recently, a high-resolution X-ray structure of the mature PSII complex has become available. Two PSII polypeptides, D1 and CP43, provide many of the ligands to an inorganic Mn 4 Ca center that is essential for water oxidation. Because of its unusual redox chemistry, PSII often undergoes degradation followed by stepwise assembly. Psb27, a small luminal polypeptide, functions as an important accessory factor in this elaborate assembly pathway. However, the structural location of Psb27 within PSII assembly intermediates has remained elusive. Here we report that Psb27 binds to CP43 in such assembly intermediates. We treated purified genetically tagged PSII assembly intermediate complexes from the cyanobacterium Synechocystis 6803 with chemical cross-linkers to examine intermolecular interactions between Psb27 and various PSII proteins. First, the water-soluble 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) was used to cross-link proteins with complementary charged groups in close association to one another. In the His27ΔctpAPSII preparation, a 58-kDa cross-linked species containing Psb27 and CP43 was identified. This species was not formed in the HT3ΔctpAΔpsb27PSII complex in which Psb27 was absent. Second, the homobifunctional thiol-cleavable cross-linker 3,3′-dithiobis(sulfosuccinimidylpropionate) (DTSSP) was used to reversibly cross-link Psb27 to CP43 in His27ΔctpAPSII preparations, which allowed the use of liquid chromatography/tandem MS to map the cross-linking sites as

show abstract

Section: Discussionmentioning

confidence: 99%

“…Three-dimensional solution structures of Psb27 were recently determined by using NMR spectroscopy (9,10). The structural arrangement of Psb27 within the PS II assembly complex, however, remains unclear.…”

Section: ↔Cp43dmentioning

confidence: 99%

Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates

Liu¹,

Huang

Chen

et al. 2011

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

View full text Add to dashboard Cite

show abstract

“…This difference in location may, in part, be responsible for functional differences of PSB27 in the two groups of organisms. In cyanobacteria, the membrane-bound PSB27 facilitates the assembly of the manganese cluster of PSII (34)(35)(36)(37)(38) by interacting tightly with the CP43 core protein in the assembly of intermediates. In land plants, on the other hand, PSB27 functions in acclimation to changing light.…”

Section: Mutant Line Accumulates Less Anthocyanin and Produces More Rosmentioning

confidence: 99%

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Hou

Garcia

et al. 2015

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

View full text Add to dashboard Cite

In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation. In response to high light exposure, the mutant plants also displayed enhanced ROS production, leading to decreased biosynthesis of anthocyanin. Unexpectedly, we detected a second defect in the mutant, namely in CP26, an antenna protein known to be required for the formation of PSII SCs that has been linked to state transitions. Lack of PSII SCs was found to be independent of PSB27, but was due to a mutation in the previously described cp26 gene that we found had no effect on light adaptation. The present results suggest that PSII SCs, despite being required for state transitions, are not associated with acclimation to changing light intensity. Our results are consistent with the conclusion that PSB27 plays an essential role in enabling plants to adapt to fluctuating light intensity through a mechanism distinct from photosystem II supercomplexes and state transitions.photosystem | PSII supercomplex | photosynthesis | anthocyanin biosynthesis | reactive oxygen species P hotosynthetic light reactions entail the coordinated function of several large membrane complexes: photosystem I (PSI), photosystem II (PSII), cytochrome b6f complex, and CF 0 -CF 1 complex. PSII catalyzes the initial step of photosynthesis, the light-dependent oxidation of water that yields molecular oxygen and reduced plastoquinone. The native form of PSII residing in the thylakoid membrane is believed to be organized into several types of supercomplexes (SCs), including the PSII core and the peripheral light harvesting complex II (LHCII), that play a primary role in the harvesting of light, transfer of excitation energy to the reaction center and regulation of light utilization. Several monomeric antenna proteins including CP24, CP26, and CP29 regulate the interaction of the PSII core with LHCII trimers (1-4). Regulation is achieved through photoprotective mechanisms that dissipate absorbed excess energy as heat in response to stress conditions such as high light intensity (5, 6).In natural settings, both the intensity and the spectral quality of light vary extensively, sometimes within very short periods. The changes in light intensity result in imbalanced excitation of PSI and PSII, and with that may lower the efficiency of the photosynthetic light reactions. In acclimating to the changing conditions, plants modify their thylakoid proteins and reorganize their photosynthetic machinery (7,8). In a rapid response, designated state transitions (9), LHCII associates...

show abstract

“…A structural NMR-based analysis of Psb27 from Synechocystis sp. strain PCC 6803 showed that it consists of a right-handed fourhelix bundle with a dipolar charge distribution (25,26), which might be important for binding to PSII at the luminal surface. In Arabidopsis thaliana, two different copies of psb27 are present.…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

Role of Novel Dimeric Photosystem II (PSII)-Psb27 Protein Complex in PSII Repair

Grasse

Mamedov

Becker

et al. 2011

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

The multisubunit membrane protein complex Photosystem II (PSII) catalyzes one of the key reactions in photosynthesis: the light-driven oxidation of water. Here, we focus on the role of the Psb27 assembly factor, which is involved in biogenesis and repair after light-induced damage of the complex. We show that Psb27 is essential for the survival of cyanobacterial cells grown under stress conditions. The combination of cold stress (30°C) and high light stress (1000 mol of photons ؋ m ؊2 ؋ s ؊1 ) led to complete inhibition of growth in a ⌬psb27 mutant strain of the thermophilic cyanobacterium Thermosynechococcus elongatus, whereas wild-type cells continued to grow. Moreover, Psb27-containing PSII complexes became the predominant PSII species in preparations from wild-type cells grown under cold stress. Two different PSII-Psb27 complexes were isolated and characterized in this study. The first complex represents the known monomeric PSII-Psb27 species, which is involved in the assembly of PSII. Additionally, a novel dimeric PSII-Psb27 complex could be allocated in the repair cycle, i.e. in processes after inactivation of PSII, by 15 N pulse-label experiments followed by mass spectrometry analysis. Comparison with the corresponding PSII species from ⌬psb27 mutant cells showed that Psb27 prevented the release of manganese from the previously inactivated complex. These results indicate a more complex role of the Psb27 protein within the life cycle of PSII, especially under stress conditions. Photosystem II (PSII)2 is the first component of the photosynthetic electron transfer chain located in the thylakoid membranes of cyanobacteria and plant chloroplasts. It catalyzes the light-driven oxidation of water to molecular oxygen (1, 2). The first organisms capable of this reaction were Gram-negative cyanobacteria that evolved 3.5 billion years ago (3).Active cyanobacterial PSII consists of 20 permanent subunits, which were identified in the x-ray structure of PSII complexes isolated from Thermosynechococcus elongatus BP-1 (henceforth T. elongatus) (4). The central D1 and D2 subunits ligate multiple cofactors that facilitate the water-splitting reaction and mediate the electron transfer to plastoquinone B (Q B ). The central antenna proteins CP43 and CP47 capture the light energy, which in turn excites the Chl D1 molecule of P680. This causes a charge separation at the primary donor with the electron subsequently transferred to pheophytin (5). After Chl D1 ϩ is reduced by P D1 , the electron is transferred from pheophytin to Q A and Q B , respectively. In turn, P D1 ϩ is rereduced by electrons from the CaMn 4 cluster and the water-splitting reaction.During the early steps of biogenesis that probably takes place in the cytoplasmic membrane (6) a PSII precomplex is formed consisting of the central heterodimer D1 and D2, cytochrome b 559 , and PsbI (7-9). This precomplex is the smallest known unit capable of charge separation. Before a functional manganese cluster can be assembled, the D1 protein that is expressed as a precursor...

show abstract

Structure of Psb27 in Solution: Implications for Transient Binding to Photosystem II during Biogenesis and Repair

Cited by 43 publications

References 16 publications

Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates

Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates

PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Role of Novel Dimeric Photosystem II (PSII)-Psb27 Protein Complex in PSII Repair

Contact Info

Product

Resources

About