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 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Japan
Oxford University Press
01-05-2008
Oxford Publishing Limited (England) |
Subjects: | |
Online Access: | Get full text |
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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. |
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Bibliography: | F60 F30 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 |