Open AccessIntramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein.
Author(s) -
Autar K. Mattoo,
Marvin Edelman
Publication year - 1987
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.84.6.1497
Subject(s) - palmitoylation , chloroplast , thylakoid , membrane protein , biology , photosystem ii , photosystem i , transport protein , biochemistry , microbiology and biotechnology , biophysics , chemistry , membrane , enzyme , cysteine , photosynthesis , gene
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.