title: Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins.
abstract: The light-harvesting complex (LHC) of barley photosystem II (PS II) was fractionated by Deriphat-polyacrylamide gel electrophoresis into five different pigmented components: one subcomplex (LHC IIb) and four pigment-proteins (LHC IIa, -c, -d, and -e). No loss of chorophyll from the components occurred during fractionation, and violaxanthin is the only photosynthetic pigment that apparently occurs in thylakoids free of association with protein. Each LHC II component has a distinct stoichiometry of neoxanthin, violaxanthin, lutein, chlorophyll a, and chlorophyll b. LHC IIa, -d, and -e were obtained as monomeric pigment-proteins, each of which contained one apoprotein Mr 31,000, 21,000, and 13,000, respectively. LHC IIc was also isolated as a monomer but it contained two poly-peptides of Mr 29,000 and 26,500, whereas the trimeric LHC IIb subcomplex (Mr 72,000) contained three subunits of Mr 28,000, 27,000, and 25,000, but not in equal stoichiometry. How the LHC II subunits are organized in PS II was examined. We isolated PS II subcomplexes which contained four of the LHC II subunits and the core complex (CC II) in unit stoichiometry; the relative strengths of association of the LHC II subunits with CC II are: LHC IIa greater than LHC IIc greater than LHC IIb greater than LHC IId. The LHC II subunits were associated with the native dimeric and not with the derived monomeric form of CC II. In addition, a multimeric LHC II sub-complex composed of the LHC IIa, LHC IIb, and LHC IId pigment-proteins was isolated. We propose that this LHC II subcomplex, which contained the Mr 28,000 and 25,000 subunits but lacked the Mr 27,000 subunit of LHC IIb and CC II. An LHC IIb pigmented fraction of LHC IIb and CC II. An LHC IIb pigmented fraction of Mr 250,000 was isolated which contained only the Mr 28,000 and 27,000 subunits. The LHC IIb subunits in this complex were the most highly phosphorylated on a protein basis. These data together with analyses of the chlorophyll b-less barley chlorina f2 mutant were used to construct a model for the LHC II pigment-protein arrangement in higher plant PS II.
authors.affiliation: Department of Biology, University of California, Los Angeles 90024-1606.
authors.forename: G F
authors.initials: GF
authors.lastname: Peter
authors.forename: J P
authors.initials: JP
authors.lastname: Thornber
mesh_terms: D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D001467:Hordeum; D045342:Light-Harvesting Protein Complexes; D046911:Macromolecular Substances; D008954:Models, Biological; D008970:Molecular Weight; D010766:Phosphorylation; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D045332:Photosystem II Protein Complex; D013057:Spectrum Analysis
chemical_list: D045342:Light-Harvesting Protein Complexes; D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex