Organization of chlorophyll-protein complexes of Photosystem I in Chlamydomonas reinhardii

Ish-Shalom, Dvorah; Ohad, Itzhak

doi:10.1016/0005-2728(83)90066-x

Cited by 68 publications

(21 citation statements)

References 27 publications

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“…In the mutant y-1 p, which lacks 4 of the polypeptides of CP0, the PSI antenna size is decreased, leading to an increase in fluorescence yield at 686 nm from ChL/b-P2. This is interpreted to mean that the four missing polypeptides form a connecting antennae between the core antenna of ChL-P1 and the light-harvesting LHCI-707 antenna, as well as Chla/b-P2 (22).…”

Section: Discussionmentioning

confidence: 99%

Chlorophyll-proteins of two photosystem I preparations from maize

Bassi

Machold

Simpson

1985

Carlsberg Res. Commun.

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Two photosystem I (PSI) preparations were purified by non-denaturing SDS-PAGE or sucrose gradient ultracentrifugation and examined as to their chlorophyll-protein composition. In both preparations a minimum of two chlorophyll-proteins can be distinguished in addition to the 110 kD P-700 Chlo-P 1 complex. One (LHCI-730) is a chlorophyll-protein (Mr 40 kD) having a high chlorophyll a/b ratio, and a major 77 K fluorescence peak at 730 nm. It consists of three polypeptides with apparent molecular weights of 21, 22.5 and 24 kD. Another chlorophyll-protein (LHCI-680) with a lower molecular weight (Mr 25 kD) fluoresces at 77 K with a maximum at 680 nm. This chlorophyll-protein has a high chlorophyll b content and two constituent polypeptides of 20 and 25 kD. Absorption, 77 K fluorescence and circular dichroism spectra of the PSI related chlorophyll-proteins are presented and compared with those of photosystem II chlorophyll-proteins from maize thylakoids. We propose a model for energy transfer in the photosystem I reaction centre with the following sequence: LHCI-730 ~ LHCI-680ChL-P 1. LHCI-680 acts as a connecting antenna which can also transfer energy from ChL/b-P2. This model was used to interpret the 77 K fluorescence emission from two barley mutants.

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Section: Discussionmentioning

confidence: 99%

Chlorophyll-proteins of two photosystem I preparations from maize

Bassi

Machold

Simpson

1985

Carlsberg Res. Commun.

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“…An interpretation of the role of two LHCI Chl alb protein moieties in C. reinhardtii CPO was proposed by Ish-Shalom and Ohad (1983), who analyzed the photosynthetic mutant (Y-1P). Polypeptide analysis showed the presence of the 27 kDa polypeptide in the absence of the other four.…”

Section: Chlorophyll Alb Proteins Of Photosystem Imentioning

confidence: 99%

CHLOROPHYLL BINDING PROTEINS WITH ANTENNA FUNCTION IN HIGHER PLANTS and GREEN ALGAE

Bassi

Rigoni

Giacometti

1990

Photochem & Photobiology

158

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“…The existence of a second light-harvesting chlorophylL/~-protein complex (LHCI) associated with photosystem I (PSI) has been recently established (3,4,5,6,7,11,12,13). Mild electrophoretic conditions yield a high molecular weight complex containing the reaction centre for PSI, the core antenna and the chlorophyll b containing light harvesting antenna.…”

Section: Introductionmentioning

confidence: 99%

Polypeptide composition of the photosystem I chlorophyll a/b -protein from three different plant species

Machold

1986

Carlsberg Res. Commun.

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Photosystem I preparations from Vicia faba, Hordeum vulgare, and Zea mays were analysed for chlorophyllo/~-binding proteins and their polypeptide composition. For this purpose the long wave-length fluorescence emitting band ChI,,/~-P3 (LHCI-730) of each species was excised from gels after electrophoresis and the concentrated eluates were subjected to denaturing re-electrophoresis. The polypeptide pattern of Chlo~-P3 obtained with gradient gels containing 6 M-urea exhibited three bands previously termed B, C, and D (3). Only a polypeptide corresponding in its migration property to D was present in the polypeptide pattern of total thylakoids. A 20 kD polypeptide which corresponds to D is missing in the chlorophyll b-less barley mutant chlorinaf2. It is concluded that D binds pigments and may represent the apoprotein of ChL/~-P3. The authenticity and function, respectively, of the polypeptidcs B and C need further elucidation.

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Organization of chlorophyll-protein complexes of Photosystem I in Chlamydomonas reinhardii

Cited by 68 publications

References 27 publications

Chlorophyll-proteins of two photosystem I preparations from maize

Chlorophyll-proteins of two photosystem I preparations from maize

CHLOROPHYLL BINDING PROTEINS WITH ANTENNA FUNCTION IN HIGHER PLANTS and GREEN ALGAE

Polypeptide composition of the photosystem I chlorophyll a/b -protein from three different plant species

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