Light Stress Proteins (Elips); The Intriguing Relatives of Cab Gene Family

Adamska, Iwona

doi:10.1007/978-94-009-0173-5_664

Cited by 3 publications

(1 citation statement)

References 10 publications

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“…Candidates that have been suggested as Chi carriers are early light-induced proteins (ELIPs) (Adamska 1997, Adamska et al 1993, also termed light-stress proteins (Adamska et al 1996), andPsbS (Funk et al 1995a,b). Both have been shown to bind Chls rather weakly (Adamska 1995, Funk et al 1994, 1995a. Interestingly, a high light-induced protein of 21 kDa localised in the envelope membrane has been suggested as a pigment carrier protein (Andreasson and Melis 1995), based on the hypothesis by Hoober et al (1994) of pigment-protein complex assembly in the envelope (see above).…”

Section: Chl-a Proteinsmentioning

confidence: 99%

Pigment ligation to proteins of the photosynthetic apparatus in higher plants

Paulsen¹

1997

Physiol Plant

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Paulsen, H. 1997. Pigment ligation to proteins of the photosynthetic apparatus in higher plants. Ligation of pigments to proteins of the thylakoid membrane is a central step in the assembly of the photosynthetic apparatus in higher plants. Because of the potentially damaging photooxidative activity of chlorophylls, it is likely that between their biosynthesis and final assembly, chlorophylls will always be bound to protein complexes in which photooxidation is prevented by quenchers such as carotenoids. Such complexes may include chlorophyll carriers and/or membrane receptors involved in protein insertion into the membrane. Many if not all pigment-protein complexes of the thylakoid are stabilised towards protease attack by bound pigments. The major light-harvesting chlorophyll a/b protein (Lhcbl,2) folds into its native structure in vitro only when it binds pigments. Pigment-induced folding may also be a general feature of chlorophyll-carotenoid proteins of the photosynthetic apparatus.

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Section: Chl-a Proteinsmentioning

confidence: 99%

Pigment ligation to proteins of the photosynthetic apparatus in higher plants

Paulsen¹

1997

Physiol Plant

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Induction of the Photosystem 2 Dark Formation in Etiolated Leaves with the Involvement of Exogenous Chlorophyllides

Domanskii¹,

Fradkin²

1999

Photosynt.

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The Chlorophyll-Carotenoid Proteins of Oxygenic Photosynthesis

Green

Durnford

1996

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

632

381

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The chlorophyll-carotenoid binding proteins responsible for absorption and conversion of light energy in oxygen-evolving photosynthetic organisms belong to two extended families: the Chl a binding core complexes common to cyanobacteria and all chloroplasts, and the nuclear-encoded light-harvesting antenna complexes of eukaryotic photosynthesizers (Chl a/b, Chl a/c, and Chl a proteins). There is a general consensus on polypeptide and pigment composition for higher plant pigment proteins. These are reviewed and compared with pigment proteins of chlorophyte, rhodophyte, and chromophyte algae. Major advances have been the determination of the structures of LHCII (major Chl a/b complex of higher plants), cyanobacterial Photosystem I, and the peridinen-Chl a protein of dinoflagellates to atomic resolution. Better isolation methods, improved transformation procedures, and the availability of molecular structure models are starting to provide insights into the pathways of energy transfer and the macromolecular organization of thylakoid membranes.

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Light Stress Proteins (Elips); The Intriguing Relatives of Cab Gene Family

Cited by 3 publications

References 10 publications

Pigment ligation to proteins of the photosynthetic apparatus in higher plants

Pigment ligation to proteins of the photosynthetic apparatus in higher plants

Induction of the Photosystem 2 Dark Formation in Etiolated Leaves with the Involvement of Exogenous Chlorophyllides

The Chlorophyll-Carotenoid Proteins of Oxygenic Photosynthesis

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