ArticleThe Journal of biological chemistry2011
Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- A flow equilibrium of zinc in cells ofJournal of bacteriology · 2024Article
- Ion selectivity and gating behavior of the CorA-type channel Bpss1228.Frontiers in chemistry · 2022Article
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- Cation permeability in CorA family of proteins.Scientific reports · 2020Article
- The structural basis of proton driven zinc transport by ZntB.Nature communications · 2017Article
- Trace Metal Acquisition by Marine Heterotrophic Bacterioplankton with Contrasting Trophic Strategies.Applied and environmental microbiology · 2016Article
- Molecular mechanism of Mg2+-dependent gating in CorA.Nature communications · 2014Article
- A repulsion mechanism explains magnesium permeation and selectivity in CorA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport.The Biochemical journal · 2013Article
- Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
CorA is a family of divalent cation transporters ubiquitously present in bacteria and archaea. Although CorA can transport both Mg(2+) and Co(2+) almost equally well, its main role has been suggested to be that of primary Mg(2+) transporter of prokaryotes and hence the regulator of Mg(2+) homeostasis. The reason is that the affinity of CorA for Co(2+) is relatively low and thus considered non-physiological. Here, we show that Thermotoga maritima CorA (TmCorA) is incapable of regulating the Mg(2+) homeostasis and therefore cannot be the primary Mg(2+) transporter of T. maritima. Further, our in vivo experiments confirm that TmCorA is a highly selective Co(2+) transporter, as it selects Co(2+) over Mg(2+) at >100 times lower concentrations. In addition, we present data that show TmCorA to be extremely thermostable in the presence of Co(2+). Mg(2+) could not stabilize the protein to the same extent, even at high concentrations. We also show that addition of Co(2+), but not Mg(2+), specifically induces structural changes to the protein. Altogether, these data show that TmCorA has the role of being the transporter of Co(2+) but not Mg(2+). The physiological relevance and requirements of Co(2+) in T. maritima is discussed and highlighted. We suggest that CorA may have different roles in different organisms. Such functional diversity is presumably a reflection of minor, but important structural differences within the CorA family that regulate the gating, substrate selection, and transport.
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