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The Plant Cell, Vol. 13, 2539-2551, November 2001, Copyright © 2001,
American Society of Plant Biologists

HCF164 Encodes a Thioredoxin-Like Protein Involved in the Biogenesis of the Cytochrome b6f Complex in Arabidopsis

Katja Lennartza, Henning Plückena, Andreas Seidlerb, Peter Westhoffa, Nicole Bechtoldc and Karin Meierhoff1,a

a Heinrich-Heine-Universität, Institut für Entwicklungs und Molekularbiologie der Pflanzen, Universitätstrasse 1, 40225 Düsseldorf, Germany
b Ruhr-Universität Bochum, Lehrstuhl für Biochemie der Pflanzen, Universitätstrasse 150, 44780 Bochum, Germany
c Station de Génétique et de Amélioration des Plantes, Institut National de la Recherche Agronomique, 78026 Versailles Cedex, France

1 To whom correspondence should be addressed. E-mail karin.meierhoff{at}uni-duesseldorf.de; fax 49-211-81-14871

To understand the biogenesis of the plastid cytochrome b6f complex and to identify the underlying auxiliary factors, we have characterized the nuclear mutant hcf164 of Arabidopsis and isolated the affected gene. The mutant shows a high chlorophyll fluorescence phenotype and is severely deficient in the accumulation of the cytochrome b6f complex subunits. In vivo protein labeling experiments indicated that the mutation acts post-translationally by interfering with the assembly of the complex. Because of its T-DNA tag, the corresponding gene was cloned and its identity confirmed by complementation of homozygous mutant plants. HCF164 encodes a thioredoxin-like protein that possesses disulfide reductase activity. The protein was found in the chloroplast, where it is anchored to the thylakoid membrane at its lumenal side. HCF164 is closely related to the thioredoxin-like protein TxlA of Synechocystis sp PCC6803, most probably reflecting its evolutionary origin. The protein also shows a limited similarity to the eubacterial CcsX and CcmG proteins, which are required for the maturation of periplasmic c-type cytochromes. The putative roles of HCF164 for the assembly of the cytochrome b6f complex are discussed.




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