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Chloroplast Cyclophilin Is a Target Protein of Thioredoxin.
- Source :
-
Journal of Biological Chemistry . 8/22/2003, Vol. 278 Issue 34, p31848-31852. 5p. 3 Diagrams, 3 Charts, 6 Graphs. - Publication Year :
- 2003
-
Abstract
- Chloroplast cyclophilin has been identified as a potential candidate of enzymes in chloroplasts that are regulated by thioredoxin (Motohashi, K., Kondoh, A., Stumpp, M. T., and Hisabori, T. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 11224-11229). In the present study we found that the peptidyl-prolyl cis-trans isomerase activity of cyclophilin is fully inactivated in the oxidized form. Reduction of cyclophilin by thioredoxin-m recovered the isomerase activity. Two crucial disulfide bonds were determined by disulfide-linked peptide mapping. The relevance of these cysteines for isomerase activity was confirmed by the mutagenesis studies. Because four cysteine residues in Arabidopsis thaliana cyclophilin were conserved in the isoforms from several organisms, it appears that this redox regulation must be one of the common regulation systems of cyclophilin. [ABSTRACT FROM AUTHOR]
- Subjects :
- *CYCLOPHILINS
*CHLOROPLASTS
*THIOREDOXIN
Subjects
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 278
- Issue :
- 34
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 10890594
- Full Text :
- https://doi.org/10.1074/jbc.M304258200