Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein.
The 32-kDa herbicide-binding protein, a component of photosystem II, is synthesized as a membrane-associated 33.5-kDa precursor within the chloroplast. We show that membrane attachment of the precursor and processing to the 32-kDa form occur in the unstacked stromal lamellae. Once processed, the 32-kDa protein translocates, within the thylakoids, to the topologically distinct stacked granal lamellae. Posttranslational palmitoylation of the processed 32-kDa protein is also shown to occur. This modification takes place in a membrane-protected domain and is mainly confined to the protein assembled in the granal lamellae, where functional photosystem II centers are concentrated.
D000215:Acylation; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D002734:Chlorophyll / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism*; D045342:Light-Harvesting Protein Complexes; D008715:Methionine / Q000378:metabolism; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014316:Tritium
D045342:Light-Harvesting Protein Complexes; D010169:Palmitic Acids; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D014316:Tritium; D002734:Chlorophyll; D019308:Palmitic Acid; D008715:Methionine