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The Outer Chloroplast Envelope Protein OEP16-1 for Plastid Import of NADPH:Protochlorophyllide Oxidoreductase A in Arabidopsis thaliana

Samol, Iga, Rossig, Claudia, Buhr, Frank, Springer, Armin, Pollmann, Stephan, Lahroussi, Abder, von Wettstein, Diter, Reinbothe, Christiane, Reinbothe, Steffen
Plant & cell physiology 2011 v.52 no.1 pp. 96-111
Arabidopsis thaliana, complementary DNA, etiolation, genes, genetic transformation, phenotype, photostability, point mutation, protein transport, proteins, seedlings, seeds, transfer DNA
The outer plastid envelope protein OEP16-1 was previously identified as an amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA). Reverse genetic approaches used to dissect these mutually not exclusive functions of OEP16-1 in planta have led to descriptions of different phenotypes resulting from the presence of several mutant lines in the SALK_024018 seed stock. In addition to the T-DNA insertion in the AtOEP16-1 gene, lines were purified that contain two additional T-DNA insertions and as yet unidentified point mutations. In a first attempt to resolve the genetic basis of four different lines in the SALK_024018 seed stock, we used genetic transformation with the OEP16-1 cDNA and segregation analyses after crossing out presumed point mutations. We show that AtOEP16-1 is involved in PORA precursor import and by virtue of this activity confers photoprotection onto etiolated seedlings during greening.