Psb27, a Cyanobacterial Lipoprotein, Is Involved in the Repair Cycle of Photosystem II

Nowaczyk, Marc M.; Hebeler, Romano; Schlodder, E.; Meyer, Helmut E.; Warscheid, Bettina; Rögner, Matthias

doi:10.1105/tpc.106.042671

Cited by 171 publications

(218 citation statements)

References 44 publications

(51 reference statements)

Supporting

Mentioning

202

Contrasting

Order By: Relevance

“…In cyanobacteria PSB27 is tightly associated with the thylakoid membrane via an N-terminal lipid modification that is absent in PSB27 from land plants (33). Therefore, PSB27 of Arabidopsis is present exclusively in the soluble phase of the thylakoid lumen (Fig.…”

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

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

show abstract

“…In cyanobacteria, it is an 11-kDa lipoprotein located solely on the luminal side of almost non-oxygen-evolving monomeric PSII (11,23). It prevents the premature binding of the extrinsic proteins (PsbO, PsbU, and PsbV) to facilitate the formation of the water-oxidizing CaMn 4 cluster within the repair cycle of PSII (11,24). A structural NMR-based analysis of Psb27 from Synechocystis sp.…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

“…Before a functional manganese cluster can be assembled, the D1 protein that is expressed as a precursor with a C-terminal extension of several amino acids has to be processed by the CtpA protease that is co-localized in the cytoplasmic membrane (10). After the precomplex is transferred to the thylakoids, the core antenna proteins CP43 and CP47 and several small subunits are assimilated to form an inactive PSII-Psb27 complex, which is in turn activated by incorporation of the CaMn 4 cluster and attachment of the extrinsic proteins (11). The details of the assembly model are still controversial, as the mechanism of the PSII transfer from one membrane system to the other is ambiguous.…”

Section: Photosystem II (Psii)mentioning

confidence: 99%

“…In conclusion, these results clearly show that Psb27 plays an important role in the viability of the cells under the stress conditions tested. 45 or 30°C for 48 h, and His-tagged PSII complexes were isolated by two HPLC steps as described previously (11). Five different PSII species could be isolated from cells grown at 45°C: PSII M(low) (peak 1), PSII M(high) (peak 2), PSII D(high) (peak 3), PSII D(low) (peak 4), and a small previously uncharacterized PSII fraction (peak 5) (Fig.…”

Section: Psb27 Is Essential For Photosynthetic Activity Under Stressmentioning

confidence: 99%

“…Anode buffer consisted of 50 mM Bistris (pH 7). Denaturing SDS gel electrophoresis according to Schägger and von Jagow (33) was carried out as described by Nowaczyk et al (11).…”

mentioning

confidence: 99%

See 2 more Smart Citations

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

Manganese in Biological Systems: Transport and Function

Salomon

Keren

Kanteev

et al. 2011

Patai's Chemistry of Functional Groups

View full text Add to dashboard Cite

Manganese import, transport, accumulation, sensing and control pathways are important for all organisms, and of unique importance for oxygenic photosynthetic organisms due to their role in the catalysis of water oxidation by photosystem II (PSII) complexes. In this review we will describe the general aspects of Mn biochemistry, its known roles in cellular processes and its mode of function in PSII. We will describe in detail different chemical mechanisms that have evolved to obtain and control Mn ions, especially focusing on cyanobacterial systems as an example of organisms with absolute Mn requirements that populate a wide variety of environments. We will describe the steps and mechanisms by which Mn transport is performed under Mn deficient or replete conditions. Under deficient conditions a high affinity Mn transporter is expressed and becomes functional in the cyanobacterial plasma membrane. This ATP dependent transporter must overcome a number of mechanistic problems to perform its function: bind Mn ions with high affinity and specificity at very low Mn concentrations in the possible presence of higher concentrations of similar metal ions. The Mn cluster of PSII functions within the cyanobacterial cell, yet studies suggest that it is assembled in the plasma membrane facing the periplasmic space rather than in the thylakoid membrane. The topology of the two processes, Mn transport and Mn cluster assembly, should therefore be regulated in order to insure efficient biogenesis and repair of PSII complexes. Based on the available results, we attempt to map the constraints imposed by Mn transport on PSII biogenesis events in cyanobacteria.

show abstract

Psb27, a Cyanobacterial Lipoprotein, Is Involved in the Repair Cycle of Photosystem II

Cited by 171 publications

References 44 publications

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

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

Manganese in Biological Systems: Transport and Function

Contact Info

Product

Resources

About