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Plant Cell Advance Online Publication
Published on October 5, 2007; 10.1105/tpc.107.051714

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Received March 19, 2007
Returned for revision September 13, 2007
Accepted September 19, 2007

Arabidopsis Cotyledon-Specific Chloroplast Biogenesis Factor CYO1 Is a Protein Disulfide Isomerase

Hiroshi Shimada 1*, Mariko Mochizuki 1, Kan Ogura 1, John E. Froehlich 2, Katherine W. Osteryoung 3, Yumiko Shirano 4, Daisuke Shibata 5, Shinji Masuda 1, Kazuki Mori 1, and Ken-ichiro Takamiya 1

1 Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan
2 Michigan State University–Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
3 Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824
4 Boyce Thompson Institute for Plant Research, Ithaca, New York 14853
5 Kazusa DNA Research Institute, Kisarazu, Chiba 292-0812, Japan

* To whom correspondence should be addressed. E-mail: hshimada{at}bio.titech.ac.jp.

Chloroplast development in cotyledons differs in a number of ways from that in true leaves, but the cotyledon-specific program of chloroplast biogenesis has not been clarified. The cyo1 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves. Chloroplasts develop abnormally in cyo1 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark. We isolated CYO1 by T-DNA tagging and verified that the mutant allele was responsible for the albino cotyledon phenotype by complementation. CYO1 has a C4-type zinc finger domain similar to that of Escherichia coli DnaJ. CYO1 is expressed mainly in young plants under light conditions, and the CYO1 protein localizes to the thylakoid membrane in chloroplasts. Transcription of nuclear photosynthetic genes is generally unaffected by the cyo1 mutation, but the level of photosynthetic proteins is decreased in cyo1 mutants. Recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin and renatures RNase A, indicating that CYO1 has protein disulfide isomerase activity. These results suggest that CYO1 has a chaperone-like activity required for thylakoid biogenesis in cotyledons.






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