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Plant and Cell Physiology Advance Access published online on January 2, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcn205
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

A novel nuclear-encoded protein, NDH-Dependent cyclic electron Flow 5, is essential for the accumulation of chloroplast NAD(P)H dehydrogenase complexes

Satoshi Ishida1, Atsushi Takabayashi2, Noriko Ishikawa1, Yasushi Hano1, Tsuyoshi Endo1 and Fumihiko Sato

1Graduate School of Biostudies, Kyoto University, Sakyo, Kyoto, 606-8502, Japan
2Center for Gene Research, Nagoya University, Chikusa, Nagoya, 464-8602, Japan

Corresponding author: Dr. Tsuyoshi Endo, Kyoto University Japan, Email: tuendo{at}kais.kyoto-u.ac.jp


  Abstract

The chloroplast NAD(P)H dehydrogenase (NDH) complex, which reduces plastoquinones in thylakoid membranes, is involved in photosystem I cyclic electron flow and chlororespiration. In addtion to land plants, the NDH complex is conserved in cyanobacteria. In this study, we identified a novel NDH-related gene of Arabidopsis, NDH-Dependent cyclic electron Flow 5 (NDF5, At1g55370). Post illumination increases in chlorophyll fluorescence were absent in ndf5 mutant plants, which indicated that NDF5 is essential for NDH activity. Sequence analysis did not reveal any known functional motifs in NDF5, but there was some homology in amino acid sequence between NDF5 and NDF2, a known NDH subunit. NDF5 and NDF2 homologues were present in higher plants, but not cyanobacteria. A single homologue, which had similarity to both NDF5 and NDF2, was identified in the moss Physcomitrella patens. Immunoblot analysis showed that NDF5 localizes to membrane fractions of chloroplasts. The stability of NdhH, a subunit of the NDH complex, as well as NDF5 and NDF2, was decreased in ndf5, ndf2 and double ndf2/ndf5 mutants, resulting in a loss of NDH activity in these mutants. These results indicated that both NDF5 and NDF2 have essential functions in the stabilization of the NDH complex. We propose that NDF5 and NDF2 were acquired by land plants during evolution, and that in higher plants, both NDF5 and NDF2 are critical to regulate NDH activity and the protein stability of each other, as well as the stability of additional NDH subunits.

Keywords: Cyclic electron flow - NAD(P)H dehydrogenase (NDH, EC 1.6.99.3) - Arabidopsis

(Received November 5, 2008; Accepted December 24, 2008)
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[Abstract] [Full Text] [PDF]


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