ArticleMetallomics : integrated biometal science2013
Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport.
Article in Metallomics : integrated biometal science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024Review
- The divalent metal ion exporter IhpABC is required to maintain iron homeostasis under low to moderate environmental iron conditions in the bacterium Bradyrhizobium japonicum.Molecular microbiology · 2024Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Functional Characterization of the CoApplied and environmental microbiology · 2023Article
- Bacterial hemerythrin domain-containing oxygen and redox sensors: Versatile roles for oxygen and redox signaling.Frontiers in molecular biosciences · 2022Review
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020Review
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Review
- Structure, function and evolution of the hemerythrin-like domain superfamily.Protein science : a publication of the Protein Society · 2018Article
- CuProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Nickel and cobalt resistance properties ofPeerJ · 2018Article
- Ferrous iron efflux systems in bacteria.Metallomics : integrated biometal science · 2017Review
- Zinc Resistance Mechanisms of P1B-type ATPases in Sinorhizobium meliloti CCNWSX0020.Scientific reports · 2016Article
- Transition Metal Transport in Plants and Associated Endosymbionts: Arbuscular Mycorrhizal Fungi and Rhizobia.Frontiers in plant science · 2016Review
- Diversity of the metal-transporting P1B-type ATPases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Fixating on metals: new insights into the role of metals in nodulation and symbiotic nitrogen fixation.Frontiers in plant science · 2014Review
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The P1B-ATPases are a ubiquitous family of metal transporters. These transporters are classified into subfamilies on the basis of substrate specificity, which is conferred by conserved amino acids in the last three transmembrane domains. Five subfamilies have been identified to date, and representative members of four (P1B-1 to P1B-4) have been studied. The fifth family (P1B-5), of which some members contain a C-terminal hemerythrin (Hr) domain, is less well characterized. The S. meliloti Sma1163 gene encodes for a P1B-5-ATPase, denoted Nia (Nickel-iron ATPase), that is induced by exogenous Fe(2+) and Ni(2+). The nia mutant accumulates nickel and iron, suggesting a possible role in detoxification of these two elements under free-living conditions, as well as in symbiosis, when the highest expression levels are measured. This function is supported by an inhibitory effect of Fe(2+) and Ni(2+) on the pNPPase activity, and by the ability of Nia to bind Fe(2+) in the transmembrane domain. Optical and X-ray absorption spectroscopic studies of the isolated Hr domain confirm the presence of a dinuclear iron center and suggest that this domain might function as an iron sensor.
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