Appearance of Type 1, 2, and 3 Light-Harvesting Complex II and Light-Harvesting Complex I Proteins during Light-Induced Greening of Barley (Hordeum vulgare) Etioplasts

Sigrist, Markus W.; Staehelin, L. Andrew

doi:10.1104/pp.104.1.135

Cited by 57 publications

(28 citation statements)

References 44 publications

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“…The SDS͞PAGE pattern of whole thylakoids, shown in Fig. 1B as a function of greening, agrees with earlier reports (31). 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).…”

Section: Resultssupporting

confidence: 78%

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: Resultssupporting

confidence: 78%

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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“…Similarly, in maize, a C4 plant having mesophyll and bundle-sheath cells, the expression of six individual Lkcb mRNAs was found to differ between these cell types and during greening (Sheen and Bogorad, 1986). Taken together, the protein studies (Sigrist and Staehelin, 1994) and mRNA studies (Sheen and Bogorad, 1986;White et al, 1992) are consistent with the hypothesis that a11 three types of LHCIIb polypeptide are required during early stages of plastid development.…”

Section: Discussionsupporting

confidence: 73%

“…7). These observations may result from the slow time course of greening in Ginkgo or an inability of etioplasts to fully convert to chloroplasts, as has been seen in barley (Sigrist and Staehelin, 1994). In barley studies the pattern of the larger PSII-LHCII complex of greening thylakoids failed to match the pattern seen in light-grown tissue, even after 8 d, suggesting that the synthesis and assembly of subtypes of these complexes is developmentally regulated and that 6-d-old etioplasts cannot be fully converted.…”

Section: Discussionmentioning

confidence: 98%

“…Protein studies have utilized microsequencing to identify and characterize the individual polypeptides Morishige and Thornber, 1991;Green et al, 1992) and, more recently, type-specific antibodies (Sigrist and Staehelin, 1991). The accumulation of types 1, 2, and 3 polypeptides of LHCI and LHCII during greening of etiolated barley seedlings has recently been studied using these type-specific antibodies (Sigrist and Staehelin, 1994). There was no difference in the rate of accumulation or time of appearance of each type of LHCIIb polypeptide during greening, although they did appear earlier in apical portions of the leaves than the basal segments.…”

Section: Discussionmentioning

confidence: 99%

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Light-Regulated and Organ-Specific Expression of Types 1, 2, and 3 Light-Harvesting Complex b mRNAs in Ginkgo biloba

1995

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In a prior study (E. Chinn and J. Silverthorne [1993] Plant Physiol 103: 727-732) we showed that the gymnosperm Ginkgo biloba was completely dependent on light for chlorophyll synthesis and chloroplast development and that expression of light-harvesting complex b (Lhcb) mRNAs was substantially increased by light. However, dark-grown seedlings that were transferred to constant white light took significantly longer than angiosperm seedlings to initiate a program of photomorphogenesis and the stems failed to green completely. We have prepared type-specific probes for mRNAs encoding major polypeptides of light-harvesting complex II (Lhcbl, Lhcb2, and Lhcb3) and have used these to analyze the expression of individual Lhcb mRNAs during greening. All three sequences accumulated in the top portions of dark-grown seedlings transferred to light, but, as was seen previously for total Lhcb mRNAs, there was a transient, reproducible decline in the levels of all three mRNAs after 4 d in the light. This transient decrease in Lhcb mRNA levels was not paralleled by a decrease in Chl accumulation. By contrast, there were significantly lower levels of all three Lhcb mRNAs i n the lower portions of greening dark-grown stems as well as lower Chl levels. We conclude that although the tops of the plants have the capacity to etiolate and green, Gingko seedling stems continue a program of development into woody tissue in darkness that precludes greening when the seedlings are transferred to the light.Light plays a central role in the induction of chloroplast development and expression of nuclear-encoded chloroplast polypeptides in flowering plants (reviewed by Sundqvist and Ryberg, 1993). In particular, light is required for the synthesis and assembly of the two photosystems, termed PSI and PSII, and their associated light-harvesting complexes, LHCI and LHCII. The major components of these thylakoid membrane complexes are the light-harvesting Chl alb-binding proteins that serve to bind Chls a and b as well as other accessory pigments such as carotenoids (Thornber et al., 1994). The best-characterized members of this superfamily of related polypeptides are the LHCIIb

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“…Whereas the Lhca2, Lhcbl, and Lhcb2 antibodies gave a signal from a single band and LhcbS from a doublet as expected (Falbel and Staehelin, 1992;Staehelin, 1992, 1994), the Lhcb3 antibody decorated three proteins. This was in contrast to a previous study (Sigrist and Staehelin, 1994), in which only one protein was detected. The middle band corresponds in size to Lhcb3 and the other two bands (30 and 22 kD) might be crossreacting proteins or posttranslational modification products.…”

contrasting

confidence: 55%

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

Krol¹,

Spangfort²,

Hüner³

et al. 1995

Plant Physiol.

171

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Appearance of Type 1, 2, and 3 Light-Harvesting Complex II and Light-Harvesting Complex I Proteins during Light-Induced Greening of Barley (Hordeum vulgare) Etioplasts

Cited by 57 publications

References 44 publications

Protein assembly and heat stability in developing thylakoid membranes during greening

Protein assembly and heat stability in developing thylakoid membranes during greening

Light-Regulated and Organ-Specific Expression of Types 1, 2, and 3 Light-Harvesting Complex b mRNAs in Ginkgo biloba

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

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