Assembly of the Light-Harvesting Complexes (LHCs) of Photosystem II (Monomeric LHC IIb Complexes Are Intermediates in the Formation of Oligomeric LHC IIb Complexes)

Dreyfuss, Beth Welty; Thornber, J. Philip

doi:10.1104/pp.106.3.829

Cited by 97 publications

(40 citation statements)

References 28 publications

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“…Two families of early light-inducible proteins (ELIPs) identified at 13-14 and 17-19 kDa by (32) are related to etioplast-to-chloroplast transformation (32,33). The major LHCII apoproteins are located between 25 and 28 kDa (34,35), and the fractional weight of the corresponding band rises Ϸ4.3-fold during greening ( Table 1). The assayed total protein͞lipid ratio was found to be 5 mg͞mg during greening and 6 mg͞mg for the mature green plants.…”

Section: Resultsmentioning

confidence: 99%

“…The protein͞lipid mass ratio increases only during the maturation phase (Ϸ24-48 h) in which LHCII apoproteins dominate the SDS͞PAGE, in agreement with ref. 35. The growth of certain SDS͞PAGE bands, most notably LHCII, which binds most of Chl in mature thylakoids (9), and the 18:3 fatty acid content follow a time course similar to that of the Chl accumulation.…”

Section: Discussionmentioning

confidence: 99%

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Protein assembly and heat stability in developing thylakoid membranes during greening

Kóta

Horváth

Droppa

et al. 2002

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

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The development of the thylakoid membrane was studied during illumination of dark-grown barley seedlings by using biochemical methods, and Fourier transform infrared and spin label electron paramagnetic resonance spectroscopic techniques. Correlated, gross changes in the secondary structure of membrane proteins, conformation, composition, and dynamics of lipid acyl chains, SDS͞PAGE pattern, and thermally induced structural alterations show that greening is accompanied with the reorganization of membrane protein assemblies and the protein-lipid interface. Changes in overall membrane fluidity and noncovalent proteinlipid interactions are not monotonic, despite the monotonic accumulation of chlorophyll, LHCII [light-harvesting chlorophyll a͞b-binding (polypeptides) associated with photosystem II] apoproteins, and 18:3 fatty acids that follow a similar time course with highest rates between 12-24 h of greening. The 18:3 fatty acid content increases 2.8-fold during greening. This appears to both compensate for lipid immobilization by membrane proteins and facilitate packing of larger protein assemblies. The increase in the amount of protein-solvating immobile lipids, which reaches a maximum at 12 h, is caused by 40% decrease in the membranous mean diameter of protein assemblies at constant protein͞lipid mass ratio. Alterations in the SDS͞PAGE pattern are most significant between 6 -24 h. The size of membrane protein assemblies increases Ϸ4.5-fold over the 12-48-h period, likely caused by the 2-fold gain in LHCII apoproteins. The thermal stability of thylakoid membrane proteins increases monotonically, as detected by an increasing temperature of partial protein unfolding during greening. Our data suggest that a structural coupling between major protein and lipid components develops during greening. This protein-lipid interaction is required for the development and protection of thylakoid membrane protein assemblies.barley (Hordeum vulgare) ͉ FTIR ͉ photosynthesis ͉ protein-lipid interaction ͉ spin label EPR

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Protein assembly and heat stability in developing thylakoid membranes during greening

Kóta

Horváth

Droppa

et al. 2002

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

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“…The Chl-or Zn-phe-complemented etioplast membranes in our experiments behave like thylakoid membranes at an early greening stage. In greening pea leaves, monomeric LHCII is accumulated 12-24 h prior to the appearance of trimeric complexes and then gradually disappears as the level of LHCII trimers increases (40). Consistently, when we inserted pLHCP into greening barley thylakoids at an early greening stage, without Chl or Zn-pheide added, the protease assay yielded LHCP-DP* exclusively, whereas insertions into thylakoids at later greening stages gave rise to gradually increasing amounts of trimeric LHCII as indicated by LHCP-DP.…”

Section: Discussionmentioning

confidence: 99%

Light-harvesting Chlorophyll a/b-binding Protein Stably Inserts into Etioplast Membranes Supplemented with Zn-pheophytina/b

Kuttkat¹,

Edhofer²,

Eichacker³

et al. 1997

Journal of Biological Chemistry

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Light-harvesting chlorophyll a/b-binding protein, LHCP, or its precursor, pLHCP, cannot be stably inserted into barley etioplast membranes in vitro. However, when these etioplast membranes are supplemented with the chlorophyll analogs Zn-pheophytin a/b, synthesized in situ from Zn-pheophorbide a/b and digeranyl pyrophosphate, pLHCP is inserted into a protease-resistant state. This proves that chlorophyll is the only component lacking in etioplast membranes that is necessary for stable LHCP insertion. Synthesis of Znpheophytin b alone promotes insertion of LHCP in vitro into a protease-resistant state, whereas synthesis of Znpheophytin a alone does not. Insertion of pLHCP into etioplast membranes can also be stimulated by adding chlorophyll a and chlorophyll b to the membranes, albeit at a significantly lower efficiency as compared with Zn-pheophytin a/b synthesized in situ. When pLHCP is inserted into chlorophyll-or Zn-pheophytin-supplemented etioplast membranes and then assayed with protease, only the protease digestion product indicative of the monomeric major light-harvesting chlorophyll a/b complex (LHCII) is found but not the one indicating trimeric complexes. In this respect, chlorophyll-or Znpheophytin-supplemented etioplast membranes resemble thylakoid membranes at an early greening stage: pLHCP inserted into plastid membranes from greening barley is assembled into trimeric LHCII only after more than 1 h of greening.

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“…Similarly, Allen et al (1988) found that the inner antenna proteins ( 0 2 9 and CP24) of the CD3 wheat mutant in greening experiments were less affected than the peripheral trimeric LHCII*. This hierarchy corresponds to the well-documented order of appearance of these Chl-binding proteins during development: first the RC components of PSI and PSII, followed by the minor / inner antenna proteins of PSII (CP29,CP26, and CP24), and finally LHCI and peripheral (trimeric) LHCII (Dreyfuss and Thornber, 1994;Sigrist and Staehelin, 1994;Paulsen, 1995, and refs. therein).…”

Section: Control Thylakoid Morphologymentioning

confidence: 99%

Severity of Mutant Phenotype in a Series of Chlorophyll-Deficient Wheat Mutants Depends on Light Intensity and the Severity of the Block in Chlorophyll Synthesis

1996

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Analyses of a series of allelic chlorina mutants of wheat (Triticum aestivum L.), which have partial blocks in chlorophyll (Chl) synthesis and, therefore, a limited Chl supply, reinforce the principle that Chl is required for the stable accumulation of Chl-binding proteins and that only reaction centers accumulate when the supply of Chl is severely limited. Depending on the rate of Chl accumulation (determined by the severity of the mutation) and on the rate of turnover of Chl and its precursors (determined by the environment in which the plant is grown), the mutants each reach an equilibrium of Chl synthesis and degradation. Together these mutants generate a spectrum of phenotypes. Under the harshest conditions (high illumination), plants with moderate blocks in Chl synthesis have membranes with very little Chl and Chl-proteins and membrane stacks resembling the thylakoids of the lethal xantha mutants of barley grown at low to medium light intensities (which have more severe blocks). In contrast, when grown under low-light conditions the same plants with moderate blocks have thylakoids resembling those of the wild type. The wide range of phenotypes of Chl b-deficient mutants has historically produced more confusion than enlightenment, but incomparable growth conditions can now explain the discrepancies reported in the literature.

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Assembly of the Light-Harvesting Complexes (LHCs) of Photosystem II (Monomeric LHC IIb Complexes Are Intermediates in the Formation of Oligomeric LHC IIb Complexes)

Cited by 97 publications

References 28 publications

Protein assembly and heat stability in developing thylakoid membranes during greening

Protein assembly and heat stability in developing thylakoid membranes during greening

Light-harvesting Chlorophyll a/b-binding Protein Stably Inserts into Etioplast Membranes Supplemented with Zn-pheophytina/b

Severity of Mutant Phenotype in a Series of Chlorophyll-Deficient Wheat Mutants Depends on Light Intensity and the Severity of the Block in Chlorophyll Synthesis

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