Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein.
AUTOR(ES)
Mattoo, A K
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=304461Documentos Relacionados
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