ArticleThe Journal of biological chemistry2016
Fine-tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe2+-ATPases.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025Review
- Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage andCurrent medicinal chemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- New complete genome insights into Enterobacter roggenkampii FACU2: a potential player in cadmium bio-removal.World journal of microbiology & biotechnology · 2024Article
- Bacterial Organelles in Iron Physiology.Molecular microbiology · 2024Review
- Iron-related gene mutations driving global Mycobacterium tuberculosis transmission revealed by whole-genome sequencing.BMC genomics · 2024Article
- 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
- Functional characterization of genes encoding cadmium pumping PMicrobiology spectrum · 2023Article
- Functional Characterization of the CoApplied and environmental microbiology · 2023Article
- Iron homeostasis inMicrobiology (Reading, England) · 2023Article
- Reconsidering theACS bio & med chem Au · 2022Article
- The evolving biology ofFrontiers in cellular and infection microbiology · 2022Review
- Structure and ion-release mechanism of PeLife · 2021Article
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Genome-wide identification and function analysis of HMAD gene family in cotton (Gossypium spp.).BMC plant biology · 2021Article
- Transcriptional regulator-induced phenotype screen reveals drug potentiators in Mycobacterium tuberculosis.Nature microbiology · 2021Article
- Genomic Insights Into Cadmium Resistance of a Newly Isolated, Plasmid-FreeFrontiers in microbiology · 2021Article
- Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020Review
- Bacillus subtilis Fur Is a Transcriptional Activator for the PerR-RepressedJournal of bacteriology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Little is known about iron efflux transporters within bacterial systems. Recently, the participation of Bacillus subtilis PfeT, a P1B4-ATPase, in cytoplasmic Fe(2+) efflux has been proposed. We report here the distinct roles of mycobacterial P1B4-ATPases in the homeostasis of Co(2+) and Fe(2+) Mutation of Mycobacterium smegmatis ctpJ affects the homeostasis of both ions. Alternatively, an M. tuberculosis ctpJ mutant is more sensitive to Co(2+) than Fe(2+), whereas mutation of the homologous M. tuberculosis ctpD leads to Fe(2+) sensitivity but no alterations in Co(2+) homeostasis. In vitro, the three enzymes are activated by both Fe(2+) and Co(2+) and bind 1 eq of either ion at their transport site. However, equilibrium binding affinities and activity kinetics show that M. tuberculosis CtpD has higher affinity for Fe(2+) and twice the Fe(2+)-stimulated activity than the CtpJs. These parameters are paralleled by a lower activation and affinity for Co(2+) Analysis of Fe(2+) and Co(2+) binding to CtpD by x-ray absorption spectroscopy shows that both ions are five- to six-coordinate, constrained within oxygen/nitrogen environments with similar geometries. Mutagenesis studies suggest the involvement of invariant Ser, His, and Glu residues in metal coordination. Interestingly, replacement of the conserved Cys at the metal binding pocket leads to a large reduction in Fe(2+) but not Co(2+) binding affinity. We propose that CtpJ ATPases participate in the control of steady state Fe(2+) levels. CtpD, required for M. tuberculosis virulence, is a high affinity Fe(2+) transporter involved in the rapid response to iron dyshomeostasis generated upon redox stress.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.