DAC Is Involved in the Accumulation of the Cytochrome b 6/f Complex in Arabidopsis
Author(s) -
Jianwei Xiao,
Jing Li,
Min Ouyang,
Tao Yun,
Baoye He,
Daili Ji,
Jinfang Ma,
Wei Chi,
Congming Lu,
Lixin Zhang
Publication year - 2012
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.112.204891
Subject(s) - cytochrome b6f complex , cytochrome , cytochrome b , mutant , arabidopsis , protein subunit , cytochrome f , thylakoid , biology , arabidopsis thaliana , biochemistry , cytochrome c , immunoprecipitation , chloroplast , microbiology and biotechnology , gene , enzyme , mitochondrion , mitochondrial dna
The biogenesis and assembly of photosynthetic multisubunit protein complexes is assisted by a series of nucleus-encoded auxiliary protein factors. In this study, we characterize the dac mutant of Arabidopsis (Arabidopsis thaliana), which shows a severe defect in the accumulation of the cytochrome b(6)/f complex, and provide evidence suggesting that the efficiency of cytochrome b(6)/f complex assembly is affected in the mutant. DAC is a thylakoid membrane protein with two predicted transmembrane domains that is conserved from cyanobacteria to vascular plants. Yeast (Saccharomyces cerevisiae) two-hybrid and coimmunoprecipitation analyses revealed a specific interaction between DAC and PetD, a subunit of the cytochrome b(6)/f complex. However, DAC was found not to be an intrinsic component of the cytochrome b(6)/f complex. In vivo chloroplast protein labeling experiments showed that the labeling rates of the PetD and cytochrome f proteins were greatly reduced, whereas that of the cytochrome b(6) protein remained normal in the dac mutant. DAC appears to be a novel factor involved in the assembly/stabilization of the cytochrome b(6)/f complex, possibly through interaction with the PetD protein.
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