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• W2149477901 abstract "Abstract NADPH:protochlorophyllide (Pchlide) oxidoreductase (POR) A is the only known example thus far of a nucleus-encoded plastid protein that is imported to its final destination in a substrate-dependent, Pchlide-regulated manner. Previous work has shown that the cytosolic PORA precursor (pPORA) does not utilize the general import site but uses a distinct translocon designated the Pchlide-dependent translocon complex. Here we demonstrate that a pentapeptide motif, threonine-threonine-serine-proline-glycine (TTSPG) in pPORA's transit peptide (transA), is involved in Pchlide-dependent transport. Deletion of this motif from the COOH-terminal end of transA abolished both Pchlide binding and protein import. Incorporation of the TTSPG motif into normally non-Pchlide-responsive transit sequences conferred the pigment binding properties onto the engineered chimeric precursors but was insufficient to render protein import substrate dependent. An additional motif was identified in the NH2-terminal part of transA that was needed for binding of the precursor to the Pchlide-dependent translocon complex. Point mutations of the TTSPG motif identified glycine as the Pchlide binding site. By analogy to the major light-harvesting chlorophyll a/b binding protein of photosystem II, we propose that the peptidyl carbonyl oxygen of glycine may bind directly or via a water molecule to the central Mg atom of the pigment." @default.
• W2149477901 created "2016-06-24" @default.
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• W2149477901 date "2008-04-25" @default.
• W2149477901 modified "2023-10-18" @default.
• W2149477901 title "A Pentapeptide Motif Related to a Pigment Binding Site in the Major Light-Harvesting Protein of Photosystem II, LHCII, Governs Substrate-Dependent Plastid Import of NADPH:Protochlorophyllide Oxidoreductase A " @default.
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• W2149477901 doi "https://doi.org/10.1104/pp.108.120113" @default.
• W2149477901 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2556810" @default.
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• W2149477901 hasPublicationYear "2008" @default.
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