Journal Article

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

Iga Samol, Claudia Rossig, Frank Buhr, Armin Springer, Stephan Pollmann, Abder Lahroussi, Diter von Wettstein, Christiane Reinbothe and Steffen Reinbothe

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 52, issue 1, pages 96-111
Published in print January 2011 | ISSN: 0032-0781
Published online November 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq177
The Outer Chloroplast Envelope Protein OEP16-1 for Plastid Import of NADPH:Protochlorophyllide Oxidoreductase A in Arabidopsis thaliana

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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.

Keywords: Chlorophyll biosynthesis; Photooxidative damage; Porphyrin-regulated plastid protein import; Singlet oxygen.

Journal Article.  8659 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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