Plant and Cell Physiology Advance Access published online on April 3, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn058
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CRR23/NdhL is a subunit of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
1Graduate School of Agriculture, Kyushu University, Higashi-ku, Fukuoka, 812-8581 Japan
2Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-85021 Japan
3Plant Genomic Network Research Team, RIKEN Plant Science Center, Tsurumi-ku, Yokohama 203-0045 Japan
4Faculty of Agriculture, University of Shizuoka, Suruga-ku, Shizuoka 422-8529 Japan
Corresponding author: Prof. Toshiharu Shikanai, Department of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502 Japan, E-mail: shikanai{at}pmg.bot.kyoto-u.ac.jp; Fax, +81-75-753-4257
| Abstract |
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The chloroplast NAD(P)H dehydrogenase (NDH) complex functions in photosystem I cyclic and chlororespiratory electron transport in higher plants. Eleven plastid-encoded and three nuclear-encoded subunits have been identified so far, but the entire subunit composition, especially of the putative electron-donor-binding module, is unclear. We isolated Arabidopsis thaliana crr23 (chlororespiratory reduction) mutants lacking NDH activity according to the absence of a transient increase in Chl fluorescence after actinic light illumination. Although CRR23 shows similarity to the NdhL subunit of cyanobacterial NDH-1, it has three transmembrane domains rather than the two in cyanobacterial NdhL. Unlike cyanobacterial NdhL, CRR23 is essential for stabilizing the NDH complex, which in turn is required for the accumulation of CRR23. Furthermore, CRR23 and NdhH, a subunit of chloroplast NDH, co-localized in blue-native gel. All the results indicate that CRR23 is an ortholog of cyanobacterial ndhL in Arabidopsis, despite its diversity of structure and function.
Keywords: NAD(P)H dehydrogenase - cyclic electron transport - photosynthesis - chloroplast - Arabidopsis
(Received February 29, 2008; Accepted April 1, 2008)
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