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Structural Insights into Iron Ions Accumulation in Dps Nanocage

Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate c...

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Autores principales: Chesnokov, Yury, Mozhaev, Andrey, Kamyshinsky, Roman, Gordienko, Alexander, Dadinova, Liubov
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9140674/
https://www.ncbi.nlm.nih.gov/pubmed/35628121
http://dx.doi.org/10.3390/ijms23105313
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author Chesnokov, Yury
Mozhaev, Andrey
Kamyshinsky, Roman
Gordienko, Alexander
Dadinova, Liubov
author_facet Chesnokov, Yury
Mozhaev, Andrey
Kamyshinsky, Roman
Gordienko, Alexander
Dadinova, Liubov
author_sort Chesnokov, Yury
collection PubMed
description Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate clusters of ferric ions in its nanocages, thus providing the bacterium with physical and chemical protection. Here, cryo-electron microscopy was used to study the accumulation of iron ions in the nanocage of a Dps protein from Escherichia coli. We demonstrate that Fe(2+) concentration in the solution and incubation time have an insignificant effect on the volume and the morphology of iron minerals formed in Dps nanocages. However, an increase in the Fe(2+) level leads to an increase in the proportion of larger clusters and the clusters themselves are composed of discrete ~1–1.5 nm subunits.
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spelling pubmed-91406742022-05-28 Structural Insights into Iron Ions Accumulation in Dps Nanocage Chesnokov, Yury Mozhaev, Andrey Kamyshinsky, Roman Gordienko, Alexander Dadinova, Liubov Int J Mol Sci Article Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate clusters of ferric ions in its nanocages, thus providing the bacterium with physical and chemical protection. Here, cryo-electron microscopy was used to study the accumulation of iron ions in the nanocage of a Dps protein from Escherichia coli. We demonstrate that Fe(2+) concentration in the solution and incubation time have an insignificant effect on the volume and the morphology of iron minerals formed in Dps nanocages. However, an increase in the Fe(2+) level leads to an increase in the proportion of larger clusters and the clusters themselves are composed of discrete ~1–1.5 nm subunits. MDPI 2022-05-10 /pmc/articles/PMC9140674/ /pubmed/35628121 http://dx.doi.org/10.3390/ijms23105313 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Chesnokov, Yury
Mozhaev, Andrey
Kamyshinsky, Roman
Gordienko, Alexander
Dadinova, Liubov
Structural Insights into Iron Ions Accumulation in Dps Nanocage
title Structural Insights into Iron Ions Accumulation in Dps Nanocage
title_full Structural Insights into Iron Ions Accumulation in Dps Nanocage
title_fullStr Structural Insights into Iron Ions Accumulation in Dps Nanocage
title_full_unstemmed Structural Insights into Iron Ions Accumulation in Dps Nanocage
title_short Structural Insights into Iron Ions Accumulation in Dps Nanocage
title_sort structural insights into iron ions accumulation in dps nanocage
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9140674/
https://www.ncbi.nlm.nih.gov/pubmed/35628121
http://dx.doi.org/10.3390/ijms23105313
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