Controlled modulation of the dynamics of the <i>Deinococcus grandis</i><scp>Dps N</scp>‐terminal tails by divalent metals

Guerra, João P. L.; Blanchet, Clément E.; Vieira, Bruno J. C.; Waerenborgh, J.C.; Jones, Nykola C.; Hoffmann, Søren Vrønning; Tavares, Pedro

doi:10.1002/pro.4567

Cited by 2 publications

(1 citation statement)

References 47 publications

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“…Besides Fe, Dps proteins are also able to bind to other transition metals [ 6 , 25 , 26 ]. Mn 2+ , Zn 2+ , Co 2+ and Cu 2+ have been found bound to the FOC with moderate affinity in different Dps homologs [ 27 , 28 , 29 , 30 ].…”

Section: Introductionmentioning

confidence: 99%

Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus

Guerra

Penas

Tavares

2023

IJMS

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Dps proteins (DNA-binding proteins from starved cells) are multifunctional stress defense proteins from the Ferritin family expressed in Prokarya during starvation and/or acute oxidative stress. Besides shielding bacterial DNA through binding and condensation, Dps proteins protect the cell from reactive oxygen species by oxidizing and storing ferrous ions within their cavity, using either hydrogen peroxide or molecular oxygen as the co-substrate, thus reducing the toxic effects of Fenton reactions. Interestingly, the interaction between Dps and transition metals (other than iron) is a known but relatively uncharacterized phenomenon. The impact of non-iron metals on the structure and function of Dps proteins is a current topic of research. This work focuses on the interaction between the Dps from Marinobacter nauticus (a marine facultative anaerobe bacterium capable of degrading petroleum hydrocarbons) and the cupric ion (Cu2+), one of the transition metals of greater biological relevance. Results obtained using electron paramagnetic resonance (EPR), Mössbauer and UV/Visible spectroscopies revealed that Cu2+ ions bind to specific binding sites in Dps, exerting a rate-enhancing effect on the ferroxidation reaction in the presence of molecular oxygen and directly oxidizing ferrous ions when no other co-substrate is present, in a yet uncharacterized redox reaction. This prompts additional research on the catalytic properties of Dps proteins.

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Section: Introductionmentioning

confidence: 99%

Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus

Guerra

Penas

Tavares

2023

IJMS

Self Cite

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Controlled modulation of the dynamics of the Deinococcus grandisDps N‐terminal tails by divalent metals

et al. 2023

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DNA‐binding proteins from starved cells (Dps) are small multifunctional nanocages expressed by prokaryotes in acute oxidative stress conditions or during the starvation‐induced stationary phase, as a bacterial defense mechanism. Dps proteins protect bacterial DNA from damage by either direct binding or by removing precursors of reactive oxygen species from solution. The DNA‐binding properties of most Dps proteins studied so far are related to their unordered, flexible, N‐ and C‐terminal extensions. In a previous work, we revealed that the N‐terminal tails of Deinoccocus grandis Dps shift from an extended to a compact conformation depending on the ionic strength of the buffer and detected a novel high‐spin ferrous iron center in the proximal ends of those tails. In this work, we further explore the conformational dynamics of the protein by probing the effect of divalent metals binding to the tail by comparing the metal‐binding properties of the wild‐type protein with a binding site‐impaired D34A variant using size exclusion chromatography, dynamic light scattering, synchrotron radiation circular dichroism, and small‐angle X‐ray scattering. The N‐terminal ferrous species was also characterized by Mössbauer spectroscopy. The results herein presented reveal that the conformation of the N‐terminal tails is altered upon metal binding in a gradual, reversible, and specific manner. These observations may point towards the existence of a regulatory process for the DNA‐binding properties of Dps proteins through metal binding to their N‐ and/or C‐terminal extensions.

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Controlled modulation of the dynamics of the Deinococcus grandisDps N‐terminal tails by divalent metals

Cited by 2 publications

References 47 publications

Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus

Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus

Controlled modulation of the dynamics of the Deinococcus grandisDps N‐terminal tails by divalent metals

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