CRR23/NdhL is a subunit of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis

The chloroplast NAD(P)H dehydrogenase (NDH) complex functions in PSI 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-...

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Published in:Plant and cell physiology Vol. 49; no. 5; pp. 835 - 842
Main Authors: Shimizu, H.(Kyushu Univ., Fukuoka (Japan)), Peng, L, Myouga, F, Motohashi, R, Shinozaki, K, Shikanai, T
Format: Journal Article
Language:English
Published: Japan Oxford University Press 01-05-2008
Oxford Publishing Limited (England)
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Summary:The chloroplast NAD(P)H dehydrogenase (NDH) complex functions in PSI 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.
Bibliography:F60
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F62
2008006688
ArticleID:pcn058
ark:/67375/HXZ-VRPVC7C7-T
istex:5DA0514E8017F5111B5ECB20F6F67E8921DACC5B
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0032-0781
1471-9053
DOI:10.1093/pcp/pcn058