Chloroplast lamellar proteins of the plastid mutant en:viridis-1 of Antirrhinum majus having impaired photosystem II

Herrmann, F.

doi:10.1016/0014-4827(72)90162-0

Cited by 28 publications

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“…One band has been observed at 50kD by many authors [6,7,9,13,15,22,24,30,34] but not in reference [26]. Some proteins between 30 kD and 40 kD have also been associated with PS 2 reaction center [10,3,13,6,22,15,9,8] ; the present work on fraction 2 is in agreement with these results.…”

Section: Resultssupporting

confidence: 82%

Protein identification of purified particles isolated from spinach thylakoids by deoxycholate electrophoresis

et al. 1982

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Three thylakoid complexes were isolated by deoxycholate preparative electrophoresis. The protein composition of each fraction was analyzed by SDS analytical electrophoresis. No protein of the PS 1 enriched fraction (fraction 1) was found in the PS 2 enriched fraction (fraction 2) and inversely. The antenna complex (fraction 3) did not have any contamination by proteins of fraction 1 or fraction 2. Fraction 1 was mainly composed of the CP1, the reaction center complex of the PS1, and by low molecular weight proteins, previously found in other PS 1 preparations. Tentative assignments of these proteins are presented; among them are iron sulfur proteins. After analytical SDS electrophoresis of fraction 2, the reaction center complex was dissociated. Nevertheless three proteins of 50 kD, 42 kD and 35 kD were assigned to this complex. Fraction 2 contained also the three cytochromes of the thylakoid membranes: cyt f, cyt b6, cyt b559. Fraction 3 was exclusively composed of one protein pigment complex, CP2.

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Section: Resultssupporting

confidence: 82%

Protein identification of purified particles isolated from spinach thylakoids by deoxycholate electrophoresis

et al. 1982

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“…Sci. USA 72 (1975) 18 (Figs. 1 and 3b) was not seen in other experiments and therefore must be due to contaminating polypeptides present in this particular experiment.…”

Section: Resultsmentioning

confidence: 99%

“…The polypeptide components of these subchloroplastic fragments or pigmentprotein complexes can then be identified by sodium dodecyl sulfate-gel electrophoresis. Another approach is to analyze the membrane polypeptides of mutant strains which are either pigment-deficient (12-16) or have specific lesions in the electron transport pathway (6,17,18). The missing or altered Abbreviations: WT, wild-type; PS I, photosystem I; PS II, photosystem II; DCMU, 3,4-dichlorophenyl dimethylurea; PBQ, p-benzoquinone; DPIP,2,6-dichlorophenol indophenol; MV, methyl viologen; HEPES, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid.…”

Section: Introductionmentioning

confidence: 99%

Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in photosystem II reaction center.

Chua¹,

Bennoun²

1975

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

451

224

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Unstacked thylakoid membrane vesicles were obtained from a homogenate of Chlamydomonas reinhardtii by flotation in a 1.8 M sucrose layer containing 5 mM HEPES (N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid)-10 mM EDTA (pH 7.5). Sodium dodecyl sulfate-gradient gel electrophoresis showed that the wildtype membranes have a total of at least 33 polypeptides ranging in molecular weights from 68,000 to less than 10,000. The wild-type and three non-photosynthetic mutant strains were studied with respect to their photosynthetic electron transport properties, their fluorescence rise kinetics, and their membrane polypeptide compositions. The results showed a strong correlation between the presence of a membrane polypeptide (molecular weight = 47,000) and the activity of the photosystem II reaction center. This polypeptide is missing from F34 (a Mendelian mutant lacking Q, the primary electron acceptor of photosystem II), but is partially restored in a suppressed strain of F34 in which there is an incomplete recovery of photosystem II activity. In a thermosensitive mutant, T4, the same polypeptide is present in reduced amount only in cells grown at 350 but not in those grown at 250. Although the mechanisms of the photosynthetic electron transport reactions have been intensively studied, relatively little is known about the molecular architecture of the thylakoid membranes on which these reactions are localized (compare ref. 1). Chemical analysis revealed that the thylakoid membranes are made up of approximately 50% lipids and 50% proteins (2). There is evidence that there are at least 10 to 20 polypeptides of different molecular weights in these membranes (3-11).Several approaches are available for the identification of the functions of the thylakoid membrane polypeptides. One approach is to fractionate the membranes by either detergents (5, 6, 9) or passage through a French pressure cell (9, 11) into small fragments enriched in either photosystem I (PS I) or photosystem II (PS II) activities. The polypeptide components of these subchloroplastic fragments or pigmentprotein complexes can then be identified by sodium dodecyl sulfate-gel electrophoresis. Another approach is to analyze the membrane polypeptides of mutant strains which are either pigment-deficient (12-16) or have specific lesions in the electron transport pathway (6,17,18). The missing or altered Abbreviations: WT, wild-type; PS I, photosystem I; PS II, photosystem II; DCMU, 3,4-dichlorophenyl dimethylurea; PBQ, p-benzoquinone; DPIP,2,6-dichlorophenol indophenol; MV, methyl viologen; HEPES, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid. 2175de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, polypeptides can then be correlated with the deleted functions in the mutant.In this paper, we have adopted the mutant approach and compared the polypeptide profile of thylakoid membrane of wild-type Chlamydomonas reinhardtii with those of mutant strains lacking or deficient in PS II activity. Our results suggest that a membrane polypeptide of mol...

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“…It was inferred from the asymmetric distribution of the chlorophylls that complex 1 and II are associated ~'ith PSI and !I, respectively (39,46). The occurrence of these two complexes has since been confirmed in a wide variety of plants (2,3,21,(23)(24)(25)(26)35).…”

mentioning

confidence: 87%

A chlorophyll-protein complex lacking in photosystem I mutants of Chlamydomonas reinhardtii.

Chua¹,

Matlin²,

Bennoun³

1975

The Journal of Cell Biology

147

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Sodium dodecyl sulfate gel electrophoresis of unheated, detergent-solubilized thylakoid membranes of Chlamydomonas reinhardtii gives two chlorophyll-protein complexes. Chlorophyll-protein complex I (CP I) is blue-green in color and can be dissociated by heat into "free" chlorophyll and a constituent polypeptide (polypeptide 2; mol wt 66,000). Similar experiments with spinach and Chinese cabbage show that the higher plant CP I contains an equivalent polypeptide but of slightly lower molecular weight (64,000). Both polypeptide 2 and its counterpart in spinach are soluble in a 2:1 (vol/vol) mixture of chloroform-methanol. Chemical analysis reveals that C. reinhardtii CP I has a chlorophyll a to b weight ratio of about 5 and that it contains approximately 5% of the total chlorophyll and 8-9% of the total protein of the thylakoid membranes. Thus, it can be calculated that each constituent polypeptide chain is associated with eight to nine chlorophyll molecules. Attempts to measure the molecular weight of CP I by calibrated SDS gels were unsuccessful since the complex migrates anomalously in such gels. Two Mendelian mutants of C. reinhardtii, FI and F14, which lack P700 but have normal photosystem I activity, do not contain CP I or the 66,000-dalton polypeptide in their thylakoid membranes. Our results suggest that CP I is essential for photosystem I reaction center activity and that P700 may be associated with the 66,000-dalton polypeptide.

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Chloroplast lamellar proteins of the plastid mutant en:viridis-1 of Antirrhinum majus having impaired photosystem II

Cited by 28 publications

References 3 publications

Protein identification of purified particles isolated from spinach thylakoids by deoxycholate electrophoresis

Protein identification of purified particles isolated from spinach thylakoids by deoxycholate electrophoresis

Thylakoid membrane polypeptides of Chlamydomonas reinhardtii: wild-type and mutant strains deficient in photosystem II reaction center.

A chlorophyll-protein complex lacking in photosystem I mutants of Chlamydomonas reinhardtii.

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