ArticlePloS one2012
Protein stability and dynamics modulation: the case of human frataxin.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Nanobodies as tools for studying human frataxin biology.Communications biology · 2026Article
- Frataxin: from the sequence to the biological role.Biophysical reviews · 2025Review
- Altered Protein Dynamics and a More Reactive Catalytic Cysteine in a Neurodegeneration-associated UCHL1 Mutant.Journal of molecular biology · 2024Article
- Modelling Protein Plasticity: The Example of Frataxin and Its Variants.Molecules (Basel, Switzerland) · 2022Article
- A New Variant of Mutational and Polymorphic Signatures in theInfection and drug resistance · 2022Article
- A Combined Spectroscopic and In Silico Approach to Evaluate the Interaction of Human Frataxin with Mitochondrial Superoxide Dismutase.Biomedicines · 2021Article
- Molecular Details of the Frataxin-Scaffold Interaction during Mitochondrial Fe-S Cluster Assembly.International journal of molecular sciences · 2021Review
- Effects of FeInternational journal of molecular sciences · 2020Article
- A Highly Conserved Iron-Sulfur Cluster Assembly Machinery between Humans and AmoebaInternational journal of molecular sciences · 2020Article
- Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin.Scientific reports · 2019Article
- Frustration, function and folding.Current opinion in structural biology · 2018Review
- Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.Scientific reports · 2016Article
- Structural characterization of metal binding to a cold-adapted frataxin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- The role of the N-terminal tail for the oligomerization, folding and stability of human frataxin.FEBS open bio · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Frataxin (FXN) is an α/β protein that plays an essential role in iron homeostasis. Apparently, the function of human FXN (hFXN) depends on the cooperative formation of crucial interactions between helix α1, helix α2, and the C-terminal region (CTR) of the protein. In this work we quantitatively explore these relationships using a purified recombinant fragment hFXN90-195. This variant shows the hydrodynamic behavior expected for a monomeric globular domain. Circular dichroism, fluorescence, and NMR spectroscopies show that hFXN90-195 presents native-like secondary and tertiary structure. However, chemical and temperature induced denaturation show that CTR truncation significantly destabilizes the overall hFXN fold. Accordingly, limited proteolysis experiments suggest that the native-state dynamics of hFXN90-195 and hFXN90-210 are indeed different, being the former form much more sensitive to the protease at specific sites. The overall folding dynamics of hFXN fold was further explored with structure-based protein folding simulations. These suggest that the native ensemble of hFXN can be decomposed in at least two substates, one with consolidation of the CTR and the other without consolidation of the CTR. Explicit-solvent all atom simulations identify some of the proteolytic target sites as flexible regions of the protein. We propose that the local unfolding of CTR may be a critical step for the global unfolding of hFXN, and that modulation of the CTR interactions may strongly affect hFXN physiological function.
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