Thioredoxin Redox Regulates ATPase Activity of Magnesium Chelatase CHLI Subunit and Modulates Redox-Mediated Signaling in Tetrapyrrole Biosynthesis and Homeostasis of Reactive Oxygen Species in Pea Plants
Adenosine Triphosphatases
Cell Nucleus
Chlorophyll
0301 basic medicine
Molecular Sequence Data
Agrobacterium
Lyases
Aminolevulinic Acid
Genes, Plant
Plants, Genetically Modified
Enzyme Activation
Chloroplast Thioredoxins
03 medical and health sciences
Phenotype
Protein Interaction Mapping
Homeostasis
Gene Silencing
Photosynthesis
Reactive Oxygen Species
Oxidation-Reduction
Pisum sativum
Plant Proteins
DOI:
10.1104/pp.112.195446
Publication Date:
2012-03-29T00:14:18Z
AUTHORS (8)
ABSTRACT
Abstract The chloroplast thioredoxins (TRXs) function as messengers of redox signals from ferredoxin to target enzymes. In this work, we studied the regulatory impact pea (Pisum sativum) TRX-F on magnesium (Mg) chelatase CHLI subunit and enzymatic activation Mg in vitro vivo. vitro, reduced activated ATPase activity enhanced reconstituted three recombinant subunits CHLI, CHLD, CHLH combination with regulator protein GENOMES UNCOUPLED4 (GUN4). Yeast two-hybrid bimolecular fluorescence complementation assays demonstrated that physically interacts but not either other two or GUN4. vivo, virus-induced gene silencing (VIGS-TRX-F) plants did result an altered state CHLI. However, simultaneous TRX-M genes (VIGS-TRX-F/TRX-M) resulted partially fully oxidized VIGS-TRX-F/TRX-M a significant reduction 5-aminolevulinic acid synthesizing capacity well pigment content lower photosynthetic capacity. These results suggest that, can compensate for lack both TRXs act important regulators chelatase. Furthermore, expression also affects tetrapyrrole biosynthesis pathway leads accumulation reactive oxygen species, which may serve additional signal transcriptional regulation photosynthesis-associated nuclear genes.
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