Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Krol, Mariana; Spangfort, Michael D.; Hüner, Norman P. A.; Öquist, Gunnar; Gustafsson, Petter; Jansson, Stefan

doi:10.1104/pp.107.3.873

Cited by 171 publications

(100 citation statements)

References 39 publications

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“…2A), drastically reduced amount of Lhcb1 (Fig. 2B) and the lack of immunodetectable Lhcb4, and Lhcb6 polypeptides (Bossmann et al, 1997;Krol et al, 1995Krol et al, , 1999. It is also demonstrated that the content of all individual carotenoid pigments in F2 mutant chloroplasts is strongly reduced as compared to the WT (Table 1).…”

Section: Consistent With Previous Reports the Quantitative Analysis Omentioning

confidence: 87%

“…As the regulated ∆pH-and zeaxanthin-dependent NPQ is believed to occur within the LHCII antenna and depend on its oligomerization state (Horton et al 1996;Wentworth et al, 2004) the strongly reduced abundance of Lhcb proteins in the F2 mutant ( Fig. 1) (Bossmann et al, 1997;Krol et al, 1995Krol et al, , 1999 can easily explain the lower NPQ in the F2 mutant. In addition, an earlier study has demonstrated that the remaining LHCII proteins in Chlorina F2 mutant do not form trimers (Allen and Staehelin, 1991).…”

Section: Discussionmentioning

confidence: 99%

“…The mutant is deficient in Lhcb1, Lhcb4, and Lhcb6 polypeptides and has reduced amounts of Lhcb2, Lhcb3 and Lhcb5 proteins (Bossmann et al, 1997;Krol et al, 1995). The reduced amount of Lhcb proteins in the F2 mutant, which is not compensated by extra chlorophylls, results in 20 and 80% reduction of the effective antennae sizes of its PSI and PSII, respectively (Harrison et al, 1993).…”

Section: Research Articlementioning

confidence: 99%

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The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

Ivanov

Król

Zeinalov

et al. 2008

Physiol Mol Biol Plants

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Analysis of the partitioning of absorbed light energy within PSII into fractions utilized by PSII photochemistry (Ø PSII ), thermally dissipated via ∆pH-and zeaxanthin-dependent energy quenching (Ø NPQ ) and constitutive non-photochemical energy losses (Ø NO ) was performed in wild type and F2 mutant of barley. The estimated energy partitioning of absorbed light to various pathways indicated that the fraction of Ø PSII was slightly higher, while the proportion of thermally dissipated energy through Ø NPQ was 38% lower in F2 mutant than in WT. In contrast, Ø NO , i.e. the fraction of absorbed light energy dissipated by additional quenching mechanism(s) was 34% higher in F2 mutant. The increased proportion of Ø NO correlated with narrowing the temperature gap (∆T M ) between S 2/3 Q B -and S 2 Q A -charge recombinations in F2 mutant as revealed by thermoluminescence measurements. We suggest that this would result in increased probability for an alternative non-radiative P680 + Q A -radical pair recombination pathway for energy dissipation within the reaction centre of PSII (reaction center quenching) and that this additional quenching mechanism might play an important role in photoprotection when the capacity for the primary, zeaxanthin-dependent non-photochemical quenching ( Research ArticleChanges in irradiance, temperature, nutrient and water availability result in imbalances between the light energy absorbed through photochemistry and energy utilization through photosynthetic electron transport coupled to carbon, nitrogen and sulphur reduction. Such an imbalance caused by changes in irradiance and/or temperature, nutrient and water availability leads to photoinhibition of photosynthesis that may result in photodamage to the D1 reaction centre polypeptide of PSII (Krause, 1988;Aro et al., 1993). The major mechanism for thermal de-excitation of excess light energy in higher plants is currently considered to be the ∆pH-and xanthophyll-cycle dependent nonphotochemical quenching (NPQ) occurring within LHCII antenna pigment bed of PSII (Demmig-Adams and Adams, 1992;Horton et al., 1996). The role of pH-and zeaxanthin-dependent shifts in the oligomerization state of LHCII in developing the rapidly relaxing energy dependent component (qE) of NPQ is well established with qE representing the major protective mechanism against photoinhibitory damage of PSII (Horton et al., 1996; Niyogi, 1999). It has been demonstrated that trimers of LHCII exhibit the optimum level of non-photochemical energy dissipation by modulating the development of the quenched state of the complex (Wentworth et al., 2004).The redox-dependent reversible phosphorylation of light-harvesting Chl a/b-binding proteins (LHCII) is the

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Section: Consistent With Previous Reports the Quantitative Analysis Omentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Research Articlementioning

confidence: 99%

See 1 more Smart Citation

The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

Ivanov

Król

Zeinalov

et al. 2008

Physiol Mol Biol Plants

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“…Recent works on in vitro reconstitution of Lhcb proteins indicated that Lhcb proteins can retain their native structure with aberrant Chl a : b ratios in vitro (Sandon et al, 1998). These results are apparently not consistent with the observation in many Chl-b de®cient mutants lacking most of the Lhc proteins, except for Lhcb5 (Harrison and Melis, 1992;Bossman et al, 1997;Kro Â l et al, 1995). A mechanism involving Lhc-speci®c proteases (Lindahl et al, 1995;Yang et al, 1998) and/or a vesiclemediating transport system of Lhcb proteins (Hoober and Eggink, 1999) Genetic modi®cation of the antenna size might be a useful tool for future improvement in crop productivity.…”

Section: Chl B Biosynthesis Regulates Accumulation Of Lhcii and Antenmentioning

confidence: 90%

Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana

et al. 2001

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SummaryThe light-harvesting ef®ciency of a photosystem is thought to be largely dependent on its photosynthetic antenna size. It has been suggested that antenna size is controlled by the biosynthesis of chlorophyll b. To verify this hypothesis, we overexpressed the enzyme for chlorophyll b biosynthesis, chlorophyllide a oxygenase (CAO), in Arabidopsis thaliana by transforming the plant with cDNA for CAO under the control of the 35S cauli¯ower mosaic virus promoter. In the early de-etiolation phase, when the intrinsic CAO expression is very low, the chlorophyll a : b ratio was drastically decreased from 28 to 7.3, indicating that enhancement of chlorophyll b biosynthesis had been successfully achieved. We made the following observations in full-green rosette leaves of transgenic plants.(1) The chlorophyll a : b ratio was reduced from 2.85 to 2.65. (2) The ratio of the peripheral light-harvesting complexes (LHCII) to the core antenna complex (CPa) resolved with the green-gel system increased by 20%. (3) The ratio of the light-harvesting complex II apoproteins (LHCP) to 47-kDa chlorophyll a protein (CP47), which was estimated by the results of immunoblotting, increased by 40%. These results indicated that the antenna size increased by at least 10±20% in transgenic plants, suggesting that chlorophyll b biosynthesis controls antenna size. To the best of our knowledge, this is the ®rst report on enlargement of the antenna size by genetic manipulations.

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“…The enzymic reaction is light independent and occurs at the stromal side of the thylakoids using the substrates Zea or Anth, which are localized within the thylakoid membrane either in the lipid bilayer adjacent to (enzymic) proteins [12] or in pigment protein complexes, e.g. the inner antenna complexes [35] or the LHCs of PSI and II [36] or in ELIPs (early lightinduced proteins) [37]. The co-substrates of the reaction were reported to be NAD(P)H and 02 [16][17][18].…”

Section: Discussionmentioning

confidence: 99%

FAD is a further essential cofactor of the NAD(P)H and O₂‐dependent zeaxanthin‐epoxidase

1995

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dase was suggested to be associated with the stromal side of this membrane [16]. Recently, Zea epoxidation activity was attributed to isolated LHCsII [19,20].In this study we demonstrate that a further cofactor, flavin adenine dinucleotide (FAD), is involved in the NAD(P)H-and O2-dependent epoxidation of Zea. Presumable, one part of the protein-associated flavin moiety is lost during the isolation procedure of the thylakoid membranes and consequently the epoxidase activity is attenuated. Addition of FAD to the thylakoid suspensions restores the enzyme activity. A further indication for the importance of this flavin during the Zea epoxidation is the strong effect of DPI, an inhibitor of flavin-containing enzymes [21,22]. Materials and methods Plant materialSpinach plants (Spinacia oleracea L. cv. Butterfly) were cultivated in a growth chamber (10 h light, 23°C, 55% rel. humidity; 14 h dark, 15°C, 70% rel. humidity). The illumination period was started and terminated by a dawn and dusk period of 1 h. For illumination HQI-R 250 W bulbs (Osram) were used (140 pmol photons-m -2-s-%. All experiments were performed with 6-week-old leaves.

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Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Cited by 171 publications

References 39 publications

The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana

FAD is a further essential cofactor of the NAD(P)H and O₂‐dependent zeaxanthin‐epoxidase

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Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Cited by 171 publications

References 39 publications

The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

The lack of LHCII proteins modulates excitation energy partitioning and PSII charge recombination in Chlorina F2 mutant of barley

Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana

FAD is a further essential cofactor of the NAD(P)H and O2‐dependent zeaxanthin‐epoxidase

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FAD is a further essential cofactor of the NAD(P)H and O₂‐dependent zeaxanthin‐epoxidase