Light-dependent accumulation and localization of photosystem II proteins in maize.
We have raised antibodies against several major components of photosystem II. These antisera, which are directed against the apoproteins of two chlorophyll-binding proteins (CPa-1 and CPa-2), the apoprotein of light-harvesting complex II and the 33-kDa extrinsic protein of the oxygen-evolving complex, were used to examine the light regulation of photosystem II assembly in maize. The principal findings of this study are as follows. The 33-kDa protein is present in dark-grown maize and the content increases 5-10-fold upon illumination. The level of the protein is mediated at least in part by phytochrome and is independent of the accumulation of chlorophyll. In contrast, none of the three chlorophyll-binding proteins examined was detectable in leaves of maize grown in darkness or under other light regimes where chlorophyll does not accumulate. Even in the absence of photosystem II assembly, the 33-kDa protein is properly transported across the thylakoid into the lumen. However, the protein does not attach in the normal way to the inner surface of the membrane under these conditions.
D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism; D002734:Chlorophyll / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism; D003624:Darkness; D007118:Immunoassay / Q000379:methods; D008027:Light; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010834:Phytochrome / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D003313:Zea mays / Q000378:metabolism* / Q000648:ultrastructure
D002352:Carrier Proteins; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D010834:Phytochrome; D002734:Chlorophyll