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

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
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.
Research Organization:
Beltsville Agricultural Research Center, MD
OSTI ID:
6526174
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 6; ISSN PNASA
Country of Publication:
United States
Language:
English