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. 1987 Mar;84(6):1497–1501. doi: 10.1073/pnas.84.6.1497

Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein.

A K Mattoo, M Edelman
PMCID: PMC304461  PMID: 3550792

Abstract

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.

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