Isolation of pigment‐binding early light‐inducible proteins from pea

Adamska, Iwona; Roobol-Bóza, Margrit; Lindahl, Marika; Andersson, Bertil

doi:10.1046/j.1432-1327.1999.00178.x

Cited by 104 publications

(82 citation statements)

References 53 publications

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“…Recent purification of Elips from light-stressed pea leaves confirmed the theoretical expectations that these proteins bind chlorophylls (43). The predicted amino acid sequences implied that also the Seps are potential chlorophyll-binding proteins.…”

Section: Discussionmentioning

confidence: 63%

Light stress-regulated two-helix proteins in Arabidopsis thaliana related to the chlorophyll a/b-binding gene family

Heddad¹

2000

Proceedings of the National Academy of Sciences

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The chlorophyll a͞b, chlorophyll a͞c, and chlorophyll a͞a light-harvesting proteins are part of an extended gene family that also includes the transiently expressed stress proteins, the Elips (early light-induced proteins). Four Elip homologue proteins, encoded by single-copy nuclear genes, have been identified in the Arabidopsis thaliana database. These proteins were divided into two groups according to the expression pattern under light-stress conditions and the predicted secondary structure. Group one included two members of the Elip family with three predicted transmembrane helices and a gene expression strictly related to light stress. Group two included two proteins, the Seps (stress-enhanced proteins), which possessed two predicted transmembrane segments. The transcripts of Sep1 and Sep2 were present under low light conditions, but their level increased 4-to 10-fold during illumination of plants with high-intensity light. Preliminary data indicated that the induced transcripts were translated in vivo. Other physiological stress conditions, such as cold, heat, desiccation, salt, wounding, or oxidative stress, did not significantly influence the expression of Sep genes. In vitro import of radioactively labeled precursors of Seps into isolated chloroplasts confirmed the thylakoid membrane localization of these proteins. Considering the predicted protein structure and homology to other pigment-antenna proteins, the two-helix Seps might represent an evolutionary missing link between the one-and three-helix antenna proteins present in pro-and eukaryota.ancestors ͉ chloroplast ͉ pigment proteins P hotosynthetic eukaryotes are traditionally divided into three major groups, largely on the basis of their light-harvesting antenna systems. The Chlorophytes (green algae and higher plants) have chlorophyll a͞b antennas, the Chromophytes have chlorophyll a͞c antennas, and the Rhodophytes (red algae) have only chlorophyll a and use phycobilisomes as the major photosystem (PS) II antenna (1, 2). The primary function of photosynthetic lightharvesting complexes is the absorption of light and the transfer of the excitation energy to the photochemical reaction centers. Because of their high sequence homology and similar structure and function, all of the eukaryotic light-harvesting antenna proteins are considered part of an extended gene family.The chlorophyll a͞b-binding (Cab) family in Arabidopsis thaliana contains at least 30 different members, associated with PSI or PSII (3). During the last few years, the Cab gene family was extended by the distant relatives, the PSII-S protein (4-6), the one-helix protein, the OHP (3), and the early light-induced proteins, the Elips (7, 8). The discovery of the cyanobacterial Hlip (high light-induced proteins) and the SCPs (small Cab-like proteins), clearly sharing the same conserved residues with the eukaryotic Cab proteins (9, 10), supported the idea that the prokaryotic Hlips and SCPs and the eukaryotic antenna proteins had a common ancestor (1, 11).The higher plant Elips are nuclear...

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Section: Discussionmentioning

confidence: 63%

Light stress-regulated two-helix proteins in Arabidopsis thaliana related to the chlorophyll a/b-binding gene family

Heddad¹

2000

Proceedings of the National Academy of Sciences

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“…Possibly, ELIPs could bind the newly formed chlorophyll molecules and could participate in their integration into the photosynthetic complexes. Accordingly, purified ELIPs have been shown to contain chlorophyll a as well as the xanthophyll lutein (8). Uncoupled chlorophyll can be detected in vivo by the lifetime of its f luorescence, which is much longer than the f luorescence lifetime of chlorophyll bound to photosynthetic complexes (29,30).…”

Section: Resultsmentioning

confidence: 99%

“…The functions of light harvesting and energy dissipation coexist within the family of LHC-type proteins (27), and this dual activity probably represented an important evolutionary step for photosynthesis in a terrestrial environment in which light can fluctuate considerably (33). The high photosensitivity of chaos indicates that thermal energy dissipation by the LHCs is not sufficient to face all the light stress conditions that vascular plants can experience in the field so that the ELIP gene and other genes coding for ancestral forms of LHCs have been preserved in the genome of green plants (8,9).…”

Section: Resultsmentioning

confidence: 99%

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Early light-induced proteins protect Arabidopsis from photooxidative stress

Hutin

Nussaume

Moise

et al. 2003

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

296

250

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The early light-induced proteins (ELIPs) belong to the multigenic family of light-harvesting complexes, which bind chlorophyll and absorb solar energy in green plants. ELIPs accumulate transiently in plants exposed to high light intensities. By using an Arabidopsis thaliana mutant (chaos) affected in the posttranslational targeting of light-harvesting complex-type proteins to the thylakoids, we succeeded in suppressing the rapid accumulation of ELIPs during high-light stress, resulting in leaf bleaching and extensive photooxidative damage. Constitutive expression of ELIP genes in chaos before light stress resulted in ELIP accumulation and restored the phototolerance of the plants to the wild-type level. Free chlorophyll, a generator of singlet oxygen in the light, was detected by chlorophyll fluorescence lifetime measurements in chaos leaves before the symptoms of oxidative stress appeared. Our findings indicate that ELIPs fulfill a photoprotective function that could involve either the binding of chlorophylls released during turnover of pigment-binding proteins or the stabilization of the proper assembly of those proteins during high-light stress.L ight is essential for plants through photosynthetic carbon assimilation. However, when absorbed light exceeds the photosynthetic capacities, reactive O 2 species are generated in the chloroplasts, causing oxidative damage to proteins, lipids, and photosynthetic pigments (1, 2). This effect is amplified by environmental stresses such as low temperature or drought, for example, that inhibit the photosynthetic activity, leading to strong yield reduction in crops. In green plants, solar energy is collected by chlorophyll-and carotenoid-binding lightharvesting complexes (LHCs), which are encoded by a multigene family of LHC genes. The expression of these genes is tightly regulated by light (2-4). High light intensities inhibit transcription of LHC genes and activate synthesis of the early lightinduced proteins (ELIPs), a class of proteins structurally related to the LHCs (5). The ELIPs are predicted to have three transmembrane helices, and they have sequence similarity to the LHCs in the central pair of helices (6, 7). The similarity is not only at the sequence level, however, because both LHCs and ELIPs bind chlorophyll and carotenoids (8). The ELIPs differ from the LHCs by their transient expression under high-light stress (5). Recently, a number of ELIP-type polypeptides, containing LHC motifs and inducible by high light, have been discovered in vascular plants: the one-helix high-light-induced proteins (9) and the two-helix stress-enhanced proteins (10).The physiological role of the ELIPs in vascular plants has not yet been elucidated, although there have been several suggestions (11)(12)(13)(14). The induction of ELIPs by high light intensities suggests a role in the acclimation to light stress rather than a light-harvesting function, but this has not yet been demonstrated. ELIP antisense transgenic tobacco plants did not exhibit any phenotype of sensitivity to high ...

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“…ATGPX7 regulates cellular photooxidative tolerance and immune responses (Chang et al, 2009). ELIP1/ELIP2 were proposed to have a photoprotective function under conditions of light stress, which they brought about by transiently binding to released chlorophyll, preventing the formation of free radicals, and participating in energy dissipation (Adamska et al, 1999;Montané and Kloppstech, 2000;Adamska et al, 2001). Overexpression of light-dependent PORA protects against photooxidative damage (Sperling et al, 1997).…”

Section: Downstream Targets Of Cych;1mentioning

confidence: 99%

CYCLIN H;1 Regulates Drought Stress Responses and Blue Light-Induced Stomatal Opening by Inhibiting Reactive Oxygen Species Accumulation in Arabidopsis

Zhou

Jin

Yoo³

et al. 2013

Plant Physiology

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Arabidopsis (Arabidopsis thaliana) CYCLIN-DEPENDENT KINASE Ds (CDKDs) phosphorylate the C-terminal domain of the largest subunit of RNA polymerase II. Arabidopsis CYCLIN H;1 (CYCH;1) interacts with and activates CDKDs; however, the physiological function of CYCH;1 has not been determined. Here, we report that CYCH;1, which is localized to the nucleus, positively regulates blue light-induced stomatal opening. Reduced-function cych;1 RNA interference (cych;1 RNAi ) plants exhibited a drought tolerance phenotype. CYCH;1 is predominantly expressed in guard cells, and its expression was substantially down-regulated by dehydration. Transpiration of intact leaves was reduced in cych;1 RNAi plants compared with the wild-type control in light but not in darkness. CYCH;1 down-regulation impaired blue light-induced stomatal opening but did not affect guard cell development or abscisic acid-mediated stomatal closure. Microarray and real-time polymerase chain reaction analyses indicated that CYCH;1 did not regulate the expression of abscisic acid-responsive genes or light-induced stomatal opening signaling determinants, such as MYB60, MYB61, Hypersensitive to red and blue1, and Protein phosphatase7. CYCH;1 down-regulation induced the expression of redox homeostasis genes, such as LIPOXYGENASE3 (LOX3), LOX4, ARABIDOPSIS GLUTATHIONE PEROXIDASE 7 (ATGPX7), EARLY LIGHT-INDUCIBLE PROTEIN1 (ELIP1), and ELIP2, and increased hydrogen peroxide production in guard cells. Furthermore, loss-of-function mutations in CDKD;2 or CDKD;3 did not affect responsiveness to drought stress, suggesting that CYCH;1 regulates the drought stress response in a CDKD-independent manner. We propose that CYCH;1 regulates blue light-mediated stomatal opening by controlling reactive oxygen species homeostasis.

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Isolation of pigment‐binding early light‐inducible proteins from pea

Cited by 104 publications

References 53 publications

Light stress-regulated two-helix proteins in Arabidopsis thaliana related to the chlorophyll a/b-binding gene family

Light stress-regulated two-helix proteins in Arabidopsis thaliana related to the chlorophyll a/b-binding gene family

Early light-induced proteins protect Arabidopsis from photooxidative stress

CYCLIN H;1 Regulates Drought Stress Responses and Blue Light-Induced Stomatal Opening by Inhibiting Reactive Oxygen Species Accumulation in Arabidopsis

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