Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase.

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Abstract Text:

Hiroshi Shimada,Mariko Mochizuki,Kan Ogura,John E Froehlich,Katherine W Osteryoung,Yumiko Shirano,Daisuke Shibata,Shinji Masuda,Kazuki Mori,Ken-Ichiro Takamiya,Hiroshi Shimada,Mariko Mochizuki,Kan Ogura,John E Froehlich,Katherine W Osteryoung,Yumiko Shirano,Daisuke Shibata,Shinji Masuda,Kazuki Mori,Ken-Ichiro Takamiya,

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 C(4)-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.

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Publishing Authors By Initials

H Shimada,M Mochizuki,K Ogura,JE Froehlich,KW Osteryoung,Y Shirano,D Shibata,S Masuda,K Mori,K Takamiya,H Shimada,M Mochizuki,K Ogura,JE Froehlich,KW Osteryoung,Y Shirano,D Shibata,S Masuda,K Mori,K Takamiya,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Plant cell

VOLUME: 19

Page Numbers: 3157-69

Journal Abbreviation: Plant Cell

ISSN: 1040-4651

DAY: 5

MONTH: 10

YEAR: 2007

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9208688

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase.

AFFILIATION: Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan. hshimada@bio.titech.ac.jp

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Plant Cell

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase Related Publications

• A simple method for extraction and partial purification of chlorophyll from plant material, using dioxane.
• Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase.
• Coronary arterial lesions of Kawasaki disease: cardiac catheterization findings of 1100 cases.
• Enzymatic properties of ubiquinol:cytochrome c2 oxidoreductase in situ in Rhodopseudomonas palustris membranes.
• Inhibitory effect of N,N'-dicyclohexylcarbodiimide (DCCD) on the electron transfer involving cytochrome b-c2 oxidoreductase in Rhodopseudomonas sphaeroides.
• Isolation of SIP, a protein that interacts with SPB, a possible transcriptional regulatory factor in Rhodobacter sphaeroides.
• NATURE OF COPPER-PROTEIN BINDING IN SPINACH PLASTOCYANIN.
• Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans.
• Purification and some properties of spinach plastocyanin.
• Structural gene of cytochrome b-562 from the cytochrome b-c1 complex of Rhodobacter sphaeroides.
• The bacterial stringent response, conserved in chloroplasts, controls plant fertilization.
• The role of plastocyanin in photoreduction of indigo carmine in chloroplasts.
• Trimethylamine N-oxide respiration by aerobic photosynthetic bacterium, Erythrobacter sp. OCh 114.