The Absence of Thioredoxin m1 and Thioredoxin C in Anabaena sp. PCC 7120 Leads to Oxidative Stress. (8th August 2018)

• Record Type: Journal Article
• Authors: Deschoenmaeker, Fr�d�ric; Mihara, Shoko; Niwa, Tatsuya; Taguchi, Hideki; Wakabayashi, Ken-Ichi; Hisabori, Toru
• Is Part Of: Plant & cell physiology. Volume 59:Number 12(2018)
• Page Start: 2432
• Page End: 2441
• Publication Date: 2018-08-08
• Subjects: 2-Cys peroxiredoxin -- NADPH-thioredoxin reductase C -- Redox regulation -- Thioredoxin; Plant physiology -- Periodicals; Microbiology -- Periodicals; Cytology -- Periodicals; Cell Physiology -- Periodicals; Plant Physiological Phenomena -- Periodicals; Cytology; Microbiology; Plant physiology; Periodicals; 571.205
• DOI: 10.1093/pcp/pcy163
• Languages: English
• ISSNs: 0032-0781

Abstract

Abstract: Thioredoxin (Trx) family proteins perform redox regulation in cells, and they are involved in several other biological processes (e.g. oxidative stress tolerance). In the filamentous cyanobacterium Anabaena sp. PCC7120 (A. 7120), eight Trx isoforms have been identified via genomic analysis. Among these Trx isoforms, the absence of Trx- m 1 and TrxC appears to result in oxidative stress in A. 7120 together with alterations of the thylakoid membrane structure and phycobiliprotein composition. To analyze the physiological changes in these Trx disruptants thoroughly, quantitative proteomics was applied. Certainly, the mutants exhibited similar alterations in the proteome including decreased relative abundance of phycobiliproteins and an increased level of proteins involved in amino acid and carbohydrate metabolism. Nevertheless, the results also indicated that the mutants exhibited changes in the relative abundance of different sets of proteins participating in reactive oxygen species detoxification, such as Fe-SOD in Δ trx-m1 and PrxQ in Δ trxC, suggesting distinct functions of Trx- m 1 and TrxC.