Evidence That the PsbK Polypeptide Is Associated with the Photosystem II Core Antenna Complex CP43

Sugimoto, Ikuyo; Takahashi, Yuichiro

doi:10.1074/jbc.m307537200

Cited by 48 publications

(38 citation statements)

References 37 publications

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“…Cells were grown to the mid-log phase in high-salt medium (40) SDS͞PAGE and Immunoblotting. We divided the gradient into 20 fractions and subjected them to urea-SDS͞PAGE (43) and immunoblotting (22). We generated an antibody against CP26 using a synthetic oligopeptide (CKGTASTKVVKPSK) conjugated with a carrier protein keyhole limpet hemocyanin at a cysteine residue (Sigma Genosys).…”

Section: Methodsmentioning

confidence: 99%

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Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii

Takahashi

Iwai

Takahashi³

et al. 2006

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

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221

195

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State transition in photosynthesis is a short-term balancing mechanism of energy distribution between photosystem I (PSI) and photosystem II (PSII). When PSII is preferentially excited (state 2), a pool of mobile light-harvesting complex II (LHCII) antenna proteins is thought to migrate from PSII to PSI, but biochemical evidence for a physical association between LHCII proteins and PSI in state 2 is weak. Here, using the green alga Chlamydomonas reinhardtii, which has a high capacity for state transitions, we report the isolation of PSI-light-harvesting complex I (LHCI) supercomplexes from cells locked into state 1 and state 2. We solubilized the thylakoid membranes with a mild detergent, separated the proteins by sucrose density gradient centrifugation, and subjected gradient fractions to gel-filtration chromatography. Three LHCII polypeptides were associated with a PSI-LHCI supercomplex only in state 2; we identified them as two minor monomeric LHCII proteins (CP26 and CP29) and one previously unreported major LHCII protein type II, or LhcbM5. These three LHCII proteins, in addition to the major trimeric LHCII proteins, were phosphorylated upon transition to state 2. The corresponding phylogenetic tree indicates that among the LHCII proteins associated with PSII, these three LHCII proteins are the most similar to the LHC proteins for PSI (LHCI). Our results are important because CP26, CP29, and LhcbM5, which have been viewed as belonging solely to the PSII complex, are now postulated to shuttle between PSI and PSII during state transitions, thereby acting as docking sites for the trimeric LHCII proteins in both PSI and PSII.photoacclimation ͉ photosynthesis ͉ photosystem I n oxygen-evolving photosynthetic organisms, two types of photosystems, photosystem I (PSI) and photosystem II (PSII), operate in series in the transfer of electrons from water to NADP ϩ . The two photosystems contain their own reaction centers and light-harvesting antenna systems. The PSI lightharvesting antenna system contains light-harvesting complex I (LHCI) proteins as peripheral monomeric antennas, whereas the PSII light-harvesting antenna system contains major and minor light-harvesting complex II (LHCII) proteins as peripheral trimeric and inner monomeric antennas, respectively (see review in ref. 1). The distribution of absorbed light energy between the two photosystems is dynamically balanced, ensuring maximum efficiency for photosynthetic electron transport in changing light environments (2, 3). That balance is regulated by a process termed ''state transitions'': state 1 is induced by preferential excitation of PSI, and state 2 is induced by preferential excitation of PSII (see recent reviews in refs. 4-6). This short-term adaptation process involves thylakoid-bound protein kinase(s) that is responsible for the phosphorylation of LHCII (7,8). The activation of the kinase(s) is regulated by the redox state of the intersystem pool of plastoquinone (9) through cytochrome b 6 f complexes (10). The phospho-LHCII proteins in the PSIIenri...

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Section: Methodsmentioning

confidence: 99%

“…2A). From the top of the gradient, A-1 represents major LHCII proteins, A-2 represents the PSII core complex, and A-3 represents the PSI-LHCI supercomplex (22,23).…”

Section: Comparison Of Chlorophyll-protein Complexes In State 1 and Smentioning

confidence: 99%

Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii

Takahashi

Iwai

Takahashi³

et al. 2006

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

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221

195

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“…The heterodimer and antenna proteins are essential for binding the prosthetic groups needed for energy and electron transfer (4) as well as for binding the multitude of plastid-encoded small subunits, e.g. Psb-H, -J, -K, -L, and Psb-T, which affect the function of PSII (5)(6)(7)(8). Furthermore, plastid-encoded subunit psbZ has been shown to be required for attachment of CP26 during assembly of PSII-LHC supercomplexes, whereas the nucleusencoded subunit psbW was demonstrated to be required for RCC dimer formation (9 -11).…”

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confidence: 99%

Accumulation of the D2 Protein Is a Key Regulatory Step for Assembly of the Photosystem II Reaction Center Complex in Synechocystis PCC 6803

Komenda

Reisinger

Müller

et al. 2004

Journal of Biological Chemistry

163

164

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Accumulation of monomer and dimer photosystem (PS) II reaction center core complexes has been analyzed by two-dimensional Blue-native/SDS-PAGE in Synechocystis PCC 6803 wild type and in mutant strains lacking genes psbA, psbB, psbC, psbDIC/DII, or the psbEFLJ operon. In vivo pulse-chase radiolabeling experiments revealed that mutant cells assembled PSII precomplexes only. In ⌬psbC and ⌬psbB, assembly of reaction center cores lacking CP43 and reaction center complexes was detected, respectively. In ⌬psbA, protein subunits CP43, CP47, D2, and cytochrome b 559 were synthesized, but proteins did not assemble. Similarly, in ⌬psbD/C lacking D2, and CP43, the de novo synthesized proteins D1, CP47, and cytochrome b 559 did not form any mutual complexes, indicating that assembly of the reaction center complex is a prerequisite for assembly with core subunits CP47 and CP43. Finally, although CP43 and CP47 accumulated in ⌬psbEFLJ, D2 was neither expressed nor accumulated. We, furthermore, show that the amount of D2 is high in the strain lacking D1, whereas the amount of D1 is low in the strain lacking D2. We conclude that expression of the psbEFLJ operon is a prerequisite for D2 accumulation that is the key regulatory step for D1 accumulation and consecutive assembly of the PSII reaction center complex. The photosystem II (PSII)1 reaction center core (RCC) complex of higher plants, algae, and cyanobacteria can be subdivided into a heterodimer containing D1 and D2, the antenna proteins CP47 and CP43, and a large number of low molecular weight integral membrane proteins including the ␣ and ␤ subunits of cytochrome b 559 (␣ and ␤ cytochrome b 559 ) (1-3). The heterodimer and antenna proteins are essential for binding the prosthetic groups needed for energy and electron transfer (4) as well as for binding the multitude of plastid-encoded small subunits, e.g. Psb-H, -J, -K, -L, and Psb-T, which affect the function of PSII (5-8). Furthermore, plastid-encoded subunit psbZ has been shown to be required for attachment of CP26 during assembly of PSII-LHC supercomplexes, whereas the nucleusencoded subunit psbW was demonstrated to be required for RCC dimer formation (9 -11). The role of plastid-encoded subunits Psb-I, -M, and -N and the nucleus-encoded small subunits Psb-R, and X remains unclear. A striking feature of PSII is the fast turnover of the D1 protein that is believed to be required for PSII repair and restoration of its photochemical activity after photoinactivation (12, 13). Maintaining PSII function may require selective replacement of this central PSII subunit including an efficient apparatus to recognize inactive complexes, and remove damaged and insert a new D1 copy (5, 14, 15). Zhang et al. (16) suggested that D1 replacement in higher plants may occur cotranslationally in a PSII subcomplex consisting of at least D2 and CP47, hence eliminating the need for complete disassembly and de novo assembly from PSII subunits.Cyanobacteria are an excellent model organism to study PSII assembly. The strain used most frequently i...

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“…4 A rapid increase in P Na shrinks cerebral vascular endothelial cells, which opens the blood-brain barrier, allowing lymphocytes, complement, and cytokines to enter the brain, damage oligodendrocytes, and cause demyelination. 5 Microglial activation seems to contribute to this process. 6 Minocycline, a tetracycline derivative, has been shown to have protective effects in experimental models of central nervous system injury, including demyelinating damage.…”

Section: Disclosuresmentioning

confidence: 99%

“…The glycocalyx of glomerular endothelial cells has been shown by enzymatic degradation, 3 use of vascular endothelial growth factor antibodies to induce glomerular endothelial injury, 4,5 and mutations of the laminin ␤3 gene 6 to result in macroalbuminuria without morphologic podocyte injury, although controversy remains. 2 Basement membrane charge properties and their molecular constituents have also been reexamined and deleted, respectively, in attempts to understand further their importance.…”

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confidence: 99%

Yet Another Advance in Understanding Albuminuria?

Molitoris¹

2010

Journal of the American Society of Nephrology

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Although the clinical relevance of proteinuria, especially albuminuria, has been well documented in chronic kidney disease, 1 the quantitative mechanistic significance of different barrier components to albuminuria remains an area of considerable excitement and debate. The glomerular filtration barrier (GFB), formed by fenestrated endothelia with their glycocalyx, podocytes with their interdigitated foot processes and slit diaphragms, the subpodocyte space, and the glomerular basement membrane (GBM), has been long believed to be the major determinant of albuminuria with podocyte foot process fusion being central. 2 Multiple genetic, molecular, and morphologic lines of evidence implicate the podocyte and its slit diaphragm as playing a central role in the GFB. However, changing concepts regarding the mechanistic relevance and clinical importance of each of these individual components of the GFB have been advancing at a rapid rate.The glycocalyx of glomerular endothelial cells has been shown by enzymatic degradation, 3 use of vascular endothelial growth factor antibodies to induce glomerular endothelial injury, 4,5 and mutations of the laminin ␤3 gene 6 to result in macroalbuminuria without morphologic podocyte injury, although controversy remains. 2 Basement membrane charge properties and their molecular constituents have also been reexamined and deleted, respectively, in attempts to understand further their importance. Clearly, laminin ␤2 mutants and null mice for either laminin ␤2 or the ␣3 chain of type IV collagen demonstrate the potential role of the GBM in albuminuria. [7][8][9][10] In addition, the glomerular endothelial cell and GBM may be able to compensate for changes in the podocyte that lead to foot process fusion and loss of the heparin sulfate glycosaminoglycan and anionic charge. 11 The recent discovery of a subpodocyte space has added another dimension to the GFB, although its role in protein filtration remains unknown. 12,13 On this background, is it little wonder that a talented investigative team, with considerable experience in the area, used a new technological advancement in scanning electron microscopy in this issue of JASN to produce data that bring into question long-held beliefs regarding the structure and function of the podocyte slit diaphragm. 14 They describe the existence of heterogeneous ellipsoidal and circular pores, located in the central region of the slit diaphragm, log normally distributed with a mean diameter far greater than envisioned previously. This was accomplished with careful attention to potential fixation, imaging, and quantitative analysis artifacts, although high-pressure freezing would have been the preferred tissue preparation.Like many scientific advances challenging previously held beliefs, it is likely to be initially refuted vigorously, which is a healthy and required part of the scientific evaluation process. Pore sizes were quantified and compared between Munich Wistar Fromter (MWF) rats, known to develop albuminuria with age and develop focal glomerular s...

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Evidence That the PsbK Polypeptide Is Associated with the Photosystem II Core Antenna Complex CP43

Cited by 48 publications

References 37 publications

Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii

Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii

Accumulation of the D2 Protein Is a Key Regulatory Step for Assembly of the Photosystem II Reaction Center Complex in Synechocystis PCC 6803

Yet Another Advance in Understanding Albuminuria?

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