Thioredoxin-dependent control balances the metabolic activities of tetrapyrrole biosynthesis
Author:
Wittmann Daniel1ORCID, Sinha Neha1ORCID, Grimm Bernhard1ORCID
Affiliation:
1. Humboldt-Universität zu Berlin, Faculty of Life Science, Institute of Biology/Plant Physiology , Philippstraße 13 (Building 12), 10115 Berlin , Germany
Abstract
Abstract
Plastids are specialized organelles found in plants, which are endowed with their own genomes, and differ in many respects from the intracellular compartments of organisms belonging to other kingdoms of life. They differentiate into diverse, plant organ-specific variants, and are perhaps the most versatile organelles known. Chloroplasts are the green plastids in the leaves and stems of plants, whose primary function is photosynthesis. In response to environmental changes, chloroplasts use several mechanisms to coordinate their photosynthetic activities with nuclear gene expression and other metabolic pathways. Here, we focus on a redox-based regulatory network composed of thioredoxins (TRX) and TRX-like proteins. Among multiple redox-controlled metabolic activities in chloroplasts, tetrapyrrole biosynthesis is particularly rich in TRX-dependent enzymes. This review summarizes the effects of plastid-localized reductants on several enzymes of this pathway, which have been shown to undergo dithiol-disulfide transitions. We describe the impact of TRX-dependent control on the activity, stability and interactions of these enzymes, and assess its contribution to the provision of adequate supplies of metabolic intermediates in the face of diurnal and more rapid and transient changes in light levels and other environmental factors.
Funder
Deutsche Forschungsgemeinschaft
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference149 articles.
1. Adams, N.B.P. and Reid, J.D. (2013). The allosteric role of the AAA+Domain of ChlD protein from the magnesium chelatase ofSynechocystisSpecies PCC 6803. J. Biol. Chem. 288: 28727–28732, https://doi.org/10.1074/jbc.m113.477943. 2. Akter, S., Huang, J., Bodra, N., De Smet, B., Wahni, K., Rombaut, D., Pauwels, J., Gevaert, K., Carroll, K., Van Breusegem, F., et al. (2015). DYn-2 based identification ofArabidopsisSulfenomes. Mol. Cell. Proteomics 14: 1183–1200, https://doi.org/10.1074/mcp.m114.046896. 3. Apitz, J., Nishimura, K., Schmied, J., Wolf, A., Hedtke, B., van Wijk, K.J., and Grimm, B. (2016). Posttranslational control of ALA synthesis includes GluTR degradation by Clp protease and stabilization by GluTR-binding protein. Plant Physiol. 170: 2040–2051, https://doi.org/10.1104/pp.15.01945. 4. Apitz, J., Schmied, J., Lehmann, M.J., Hedtke, B., and Grimm, B. (2014). GluTR2 complements a hema1 mutant lacking glutamyl-tRNA reductase 1, but is differently regulated at the post-translational level. Plant Cell Physiol. 55: 645–657, https://doi.org/10.1093/pcp/pcu016. 5. Armstrong, G.A., Runge, S., Frick, G., Sperling, U., and Apel, K. (1995). Identification of NADPH:protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol. 108: 1505–1517, https://doi.org/10.1104/pp.108.4.1505.
Cited by
13 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|