| Literature DB >> 16884685 |
Jeong Chan Moon1, Ho Hee Jang, Ho Byoung Chae, Jung Ro Lee, Sun Yong Lee, Young Jun Jung, Mi Rim Shin, Hye Song Lim, Woo Sik Chung, Dae-Jin Yun, Kyun Oh Lee, Sang Yeol Lee.
Abstract
2-Cys peroxiredoxins (Prxs) play important roles in the antioxidative defense systems of plant chloroplasts. In order to determine the interaction partner for these proteins in Arabidopsis, we used a yeast two-hybrid screening procedure with a C175S-mutant of Arabidopsis 2-Cys Prx-A as bait. A cDNA encoding an NADPH-dependent thioredoxin reductase (NTR) isotype C was identified and designated ANTR-C. We demonstrated that this protein effected efficient transfer of electrons from NADPH to the 2-Cys Prxs of chloroplasts. Interaction between 2-Cys Prx-A and ANTR-C was confirmed by a pull-down experiment. ANTR-C contained N-terminal TR and C-terminal Trx domains. It exhibited both TR and Trx activities and co-localized with 2-Cys Prx-A in chloroplasts. These results suggest that ANTR-C functions as an electron donor for plastidial 2-Cys Prxs and represents the NADPH-dependent TR/Trx system in chloroplasts.Entities:
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Year: 2006 PMID: 16884685 DOI: 10.1016/j.bbrc.2006.07.088
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575