ArticlePlant signaling & behavior2014
Putative roles of glutaredoxin-BolA holo-heterodimers in plants.
Article in Plant signaling & behavior, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism-Review.Molecules (Basel, Switzerland) · 2020Review
- Is There a Role for Glutaredoxins and BOLAs in the Perception of the Cellular Iron Status in Plants?Frontiers in plant science · 2019Article
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Glutaredoxin S15 Is Involved in Fe-S Cluster Transfer in Mitochondria Influencing Lipoic Acid-Dependent Enzymes, Plant Growth, and Arsenic Tolerance in Arabidopsis.Plant physiology · 2016Article
- Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery.Biochimica et biophysica acta · 2015Review
- Fe-S proteins that regulate gene expression.Biochimica et biophysica acta · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several genomic analyses, high-throughput or targeted interaction studies including the purification of protein complexes indicated a physical and functional link between BolAs and monothiol glutaredoxins (Grxs) that is conserved both in prokaryotes and eukaryotes. In a recent work, we confirmed that several Arabidopsis protein couples, used as plant representatives, also physically interact. More interestingly, we determined that two BolA proteins, BolA2 and SufE1, contain a conserved cysteine that is sensitive to oxidizing treatments, unraveling a possible redox-control of BolA2 and SufE1 by monothiol glutaredoxins. By coexpressing physiological partners in E. coli, Grx-BolA heterodimers binding a labile, oxygen sensitive iron-sulfur cluster were isolated. Altogether, these results illustrate the existence of different modes of interaction between monothiol glutaredoxins and BolA proteins in plants and probably in other organisms. Incidentally, the function of each partner could be differentially modulated depending on the type of interaction.
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Registered trials
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