Abstract
The BolA-like protein is present in all eukaryotes, and it is able to form complex with monothiol glutaredoxin of the same subcellular compartments, suggesting that the BolA-like protein has essential function in eukaryotes, and that the function is associated with its partner glutaredoxin. Some studies have indicated a role for BolA proteins in Fe-S cluster synthesis or in redox homeostasis. However, the physiological function of BolA proteins remains to be elucidated. Here, we report the characterization of an insertion mutant of BolA3 in Arabidopsis. Among the four AtBolA proteins found in Arabidopsis, the AtBolA3 was the only BolA located in the cytosol of plant cells. It was highly expressed in roots. AtBolA3 was able to interact with the cytosolic monothiol glutaredoxin, AtGRXS17. The bola3 mutant did not show any notable phenotype under normal growth condition, but rather grew better than wild type under some stresses. The bola3 mutant was more tolerant to excess iron and the MV-induced oxidative stress than wild type. It displayed no necrosis in leaves, developed longer roots, accumulated more iron and higher Fe-S protein activities in roots. In addition, the mutant possessed a more potent antioxidant defense to scavenge ROS species. Taken together, our data indicated that the cytosolic AtBolA3 has a suppressive role in the tolerance to excess iron and the MV-induced oxidative stress in plants. AtBolA3 seems to be a repressor under some stress conditions.
Highlights
Iron is an essential micronutrient for plants, which is used for the biosynthesis of heme and iron-sulfur (Fe-S) clusters [1,2,3]
According to the recommended nomenclature, these genes were named as AtBolA1 through AtBolA4 respectively, in an order corresponding to their chromosome locations
Amino acids were highly conserved in the C-terminus of proteins, which was annotated as the BolA domain
Summary
Iron is an essential micronutrient for plants, which is used for the biosynthesis of heme and iron-sulfur (Fe-S) clusters [1,2,3]. Excess iron could be toxic to plants in acidic soil. Cytosolic BolA as a Repressor under Stress to acquire iron from soil, iron reduction strategy and iron chelation strategy, respectively [4,5,6]. The iron nutrients are transported from the root to the shoot, taken up into plant cells, and distributed into subcellular compartments, where they are used to assemble iron-containing cofactors, in particular, the Fe-S clusters [2,7]. Despite that Fe-S clusters consist of two elements, the biosynthesis of Fe-S clusters is highly complex in the living cells. As an activator of NFS2, SufE1 consists of a N-terminal SufE domain and a C-terminal domain with similarity to the bacterial BolA [9]
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