The resolution and biochemical characterization of subcomplexes of the main light-harvesting chlorophyll a/b-protein complex of Photosystem II (LHC II)

1995 ◽  
Vol 43 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Grzegorz Jackowski ◽  
Roman Przymusiński
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Biochemical Characterization ◽  
Light Harvesting ◽  
Lhc Ii

The Oligomeric Arrangement of the Light-Harvesting Chlorophyll a/6-Protein Complex of Photosystem II

1994 ◽  
Vol 49 (5-6) ◽  
pp. 337-342 ◽  
Author(s):  
Grzegorz Jackowski ◽  
Ewa Kluck
Keyword(s):  
Photosystem Ii ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Light Harvesting ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dianthus Caryophyllus ◽  
Lhc Ii ◽  
Induced Aggregation ◽  
Oligomeric Forms

Abstract The light-harvesting chlorophyll a/b-protein complex of photosystem II (LHC II) was isolated from carnation (Dianthus caryophyllus L.) leaves by K+-induced aggregation of n-hep-tylthioglucoside-treated photosystem II particles. When solubilized with a mixture of lithium docedyl sulphate, octyl-β-D-glucopyranoside and dodecyl-β-D-maltoside the LHC II was re­ solved by mild sodium dodecyl sulphate-polyacrylamide gel electrophoresis into four oligo­meric forms and a monomeric one. LHC II contained five major polypeptides only two of which (27 and 26 kDa) were found to be its authentic components. The oligomeric forms of LHC II were found to differ in the stoichiometric ratios of the polypeptides present. The 26 kD a polypeptide was enriched in the largest oligomeric forms while the 27 kDa polypep­tide tended to form a monomer or to assemble as lower oligomeric states of LHC II.

scholarly journals Monoclonal antibodies to the light-harvesting chlorophyll a/b protein complex of photosystem II.

1986 ◽  
Vol 103 (3) ◽  
pp. 733-740 ◽  
Author(s):  
S C Darr ◽  
S C Somerville ◽  
C J Arntzen
Keyword(s):  
Monoclonal Antibodies ◽  
Photosystem Ii ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Light Harvesting ◽  
Binding Studies ◽  
Lhc Ii ◽  
Intermittent Light ◽  
Common Precursor ◽  
Lhc I

A collection of 17 monoclonal antibodies elicited against the light-harvesting chlorophyll a/b protein complex which serves photosystem II (LHC-II) of Pisum sativum shows six classes of binding specificity. Antibodies of two of the classes recognize a single polypeptide (the 28- or the 26- kD polypeptides), thereby suggesting that the two proteins are not derived from a common precursor. Other classes of antibodies cross-react with several polypeptides of LHC-II or with polypeptides of both LHC-II and the light-harvesting chlorophyll a/b polypeptides of photosystem I (LHC-I), indicating that there are structural similarities among the polypeptides of LHC-II and LHC-I. The evidence for protein processing by which the 26-, 25.5-, and 24.5-kD polypeptides are derived from a common precursor polypeptide is discussed. Binding studies using antibodies specific for individual LHC-II polypeptides were used to quantify the number of antigenic polypeptides in the thylakoid membrane. 27 copies of the 26-kD polypeptide and two copies of the 28-kD polypeptide were found per 400 chlorophylls. In the chlorina f2 mutant of barley, and in intermittent light-treated barley seedlings, the amount of the 26-kD polypeptide in the thylakoid membranes was greatly reduced, while the amount of 28-kD polypeptide was apparently not affected. We propose that stable insertion and assembly of the 28-kD polypeptide, unlike the 26-kD polypeptide, is not regulated by the presence of chlorophyll b.

High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

1990 ◽  
Vol 48 (1) ◽  
pp. 610-610
Author(s):  
Werner Kühlbrandt ◽  
Da Neng Wang ◽  
K.H. Downing
Keyword(s):  
High Resolution ◽  
Electron Diffraction ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Structural Integrity ◽  
Light Harvesting ◽  
Lhc Ii ◽  
Diffraction Patterns ◽  
Difference Fourier ◽  
2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

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