Phosphorylation of spinach chlorophyll-protein complexes. CPII, but not CP29, CP27, or CP24, is phosphorylated in vitro.
Previous studies have indicated that the reversible phosphorylation of a population of antenna complexes that can donate energy to PS II ('mobile LHC II') plays a regulatory role in the state 1-state 2 transition in thylakoid membranes. The relationship of phosphorylated LHC II to the multiple PS II-associated chlorophyll a/b-proteins resolvable on green gels is currently unclear. We have used a high resolution gel system to analyze thylakoids phosphorylated in vitro. The only PS II-associated antenna complex to become phosphorylated is CPII, indicating that this complex represents the mobile LHC II. The other putative PS II antenna complexes, CP29, CP24, and the new complex designated CP27 which comigrates with CPII, are not phosphorylated and are probably components of the bound 'LHC II' antenna.
D002734:Chlorophyll / Q000378:metabolism*; D002736:Chloroplasts / Q000032:analysis; D045342:Light-Harvesting Protein Complexes; D010766:Phosphorylation; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D002734:Chlorophyll