scholarly journals Light-dependent reversal of dark-chilling induced changes in chloroplast structure and arrangement of chlorophyll–protein complexes in bean thylakoid membranes

2005 ◽  
Vol 1710 (1) ◽  
pp. 13-23 ◽  
Author(s):  
Maciej Garstka ◽  
Anna Drożak ◽  
Małgorzata Rosiak ◽  
Jan Henk Venema ◽  
Borys Kierdaszuk ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Chloroplast Structure ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Induced Changes

Arrangement of Chlorophyll Protein Complexes Determines Chloroplast Structure

2008 ◽  
pp. 791-793
Author(s):  
Rumak Izabela ◽  
Gieczewska Katarzyna ◽  
Koziol-Lipinska Joanna ◽  
Kierdaszuk Borys ◽  
Mostowska Agnieszka ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Chloroplast Structure ◽  
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.

Growth and development at cold-hardening temperatures. Chlorophyll–protein complexes and thylakoid membrane polypeptides

1984 ◽  
Vol 62 (1) ◽  
pp. 61-67 ◽  
Author(s):  
B. Elfman ◽  
N. P. A. Huner ◽  
M. Griffith ◽  
M. Krol ◽  
W. G. Hopkins ◽  
...  
Keyword(s):  
Growth And Development ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Cold Hardening ◽  
Complex Iv ◽  
Light Harvesting Complex ◽  
Dodecyl Sulfate ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein

Chlorophyll–protein complexes of thylakoid membranes from rye plants (Secale cereale L. cv. Puma) grown at warm and cold-hardening temperatures were investigated by gel electrophoresis. Complex IV from cold-grown tissue was detectable in the presence of dodecyl sulfate if and only if solubilization and electrophoresis were performed at 4 °C, whereas complex IV from warm-grown material was detectable if membrane solubilization and electrophoresis were performed at either 4 or 23 °C in the presence of dodecyl sulfate. In the presence of octyl-β-D-glucopyranoside, the chlorophyll–protein complexes from cold-grown tissue were less stable at 23 °C than those from warm-grown tissue. Regardless of the detergent used, there was always more oligomer of the light-harvesting complex present in samples prepared from thylakoid membranes of warm-grown tissue than those from membranes of cold-grown tissue. It is concluded that the pigment–protein interaction in those complexes associated with photosystem II and the light-harvesting chlorophyll a/b – protein complex has been altered upon growth and development at cold-hardening temperatures.

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