Polypeptides of chloroplastic and cytoplastic origin required for development of Photosystem II activity, and chlorophyll-protein complexes, in Euglena gracilis Z chloroplast membranes

1977 ◽  
Vol 461 (3) ◽  
pp. 475-488 ◽  
Author(s):  
Michael Gurevitz ◽  
Hanan Kratz ◽  
Itzhak Ohad
Keyword(s):  
Photosystem Ii ◽  
Euglena Gracilis ◽  
Protein Complexes ◽  
Chloroplast Membranes ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Photosystem Ii Activity ◽  
Euglena Gracilis Z

scholarly journals Chloroplast membranes of the green alga Acetabularia mediterranea. II. Topography of the chloroplast membrane.

1976 ◽  
Vol 71 (3) ◽  
pp. 876-893 ◽  
Author(s):  
K Apel ◽  
K R Miller ◽  
L Bogorad ◽  
G J Miller
Keyword(s):  
Protein Complexes ◽  
Lipid Layer ◽  
Chloroplast Membranes ◽  
Chloroplast Membrane ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Acetabularia Mediterranea ◽  
Triton X ◽  
Binding Subunit ◽  
Pronase Treatment

The localization of the chlorophyll-protein complexes inside the thylakoid membrane of Acetabularia mediterranea was determined by fractionating the chloroplast membrane with EDTA and Triton X-100, by using pronase treatment, and by labeling the surface-exposed proteins with 125I. The effects of the various treatments were established by electrophoresis of the solubilized membrane fractions and electron microscopy. After EDTA and pronase treatment, the membrane structure was still intact. Only the two chlorophyll-protein complexes of 67,000 and 152,000 daltons and an additional polypeptides were found in the membrane before the EDTA and pronase treatment. The 125,000 dalton complex seems to be buried inside the lipid layer. The 23,000 dalton subunit of the 67,000 dalton complex is largely exposed to the surface of the EDTA-insoluble membrane and only the chlorophyll-binding subunit of 21,500 daltons is buried inside the lipid layer.

A study of Photosystem II fluorescence emission in terms of the antenna chlorophyll-protein complexes

1993 ◽  
Vol 1183 (1) ◽  
pp. 194-200 ◽  
Author(s):  
Robert C. Jennings ◽  
Flavio M. Garlaschi ◽  
Roberto Bassi ◽  
Giuseppe Zucchelli ◽  
Alberto Vianelli ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Protein Complexes ◽  
Fluorescence Emission ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

scholarly journals Acyl lipids in the supramolecular chlorophyll-protein complexes of photosystems - isolation artifacts or integral components regulating their structure and functions?

2014 ◽  
Vol 57 (3) ◽  
pp. 401-418 ◽  
Author(s):  
Zbigniew Krupa
Keyword(s):  
Photosystem Ii ◽  
Lipid Content ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Supramolecular Complexes ◽  
Hexadecenoic Acid ◽  
Acyl Lipids ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Structure And Functions

The precise nature of interactions between the chloropnyll-protein complexes related to photosystem I or photosystem II and the acyl lipids in the thylakoid membranes is not yet fully elucidated. Analyses of the lipid content of isolated photosystem supramolecular complexes reveal that they are integral components of these complexes. However, the relations between certain acyl lipids and the specific structure and functions of the complexes investigated are still widely discussed. The most generally accepted phenomenon is the fact of participation of phosphatidylglycerol containing the unique <em>trans-</em>Δ<sup>3</sup> -hexadecenoic acid in the oligomerization of the light-harvesting chlorophyll a/b protein complex II.

scholarly journals Structural changes and lateral redistribution of photosystem II during donor side photoinhibition of thylakoids.

1992 ◽  
Vol 119 (2) ◽  
pp. 325-335 ◽  
Author(s):  
R Barbato ◽  
G Friso ◽  
F Rigoni ◽  
F Dalla Vecchia ◽  
G M Giacometti
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Structural Changes ◽  
Protein Complexes ◽  
Gradient Centrifugation ◽  
Photosynthetic Apparatus ◽  
Topological Stability ◽  
Donor Side ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

The structural and topological stability of thylakoid components under photoinhibitory conditions (4,500 microE.m-2.s-1 white light) was studied on Mn depleted thylakoids isolated from spinach leaves. After various exposures to photoinhibitory light, the chlorophyll-protein complexes of both photosystems I and II were separated by sucrose gradient centrifugation and analysed by Western blotting, using a set of polyclonals raised against various apoproteins of the photosynthetic apparatus. A series of events occurring during donor side photoinhibition are described for photosystem II, including: (a) lowering of the oligomerization state of the photosystem II core; (b) cleavage of 32-kD protein D1 at specific sites; (c) dissociation of chlorophyll-protein CP43 from the photosystem II core; and (d) migration of damaged photosystem II components from the grana to the stroma lamellae. A tentative scheme for the succession of these events is illustrated. Some effects of photoinhibition on photosystem I are also reported involving dissociation of antenna chlorophyll-proteins LHCI from the photosystem I reaction center.

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