Structural diffusion properties of two atypical Dps from the cyanobacterium Nostoc punctiforme disclose interactions with ferredoxins and DNA

Moparthi, Vamsi K.; Moparthi, Satish Babu; Howe, Christoph; Raleiras, Patrícia; Wenger, Jérôme; Stensjö, Karin

doi:10.1016/j.bbabio.2019.148063

Cited by 9 publications

(7 citation statements)

References 68 publications

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“…The color of the yellow band was caused by the O 2– ‐to‐Fe 3+ LMCT process, supporting that a yellow 150‐kDa band was assigned to the dodecameric structure containing iron oxyhydroxide clusters even though a smaller molecular mass was suggested by native PAGE (calculated mass of Tl Dps1 without metal cations was 248 kDa). A similar result was also observed in Np Dps4 [35]. In this report, an ~ 160‐kDa band of the putative dodecamer of Np Dps4 (262 kDa) was observed via native PAGE.…”

Section: Resultssupporting

confidence: 87%

Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites

et al. 2020

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Section: Resultssupporting

confidence: 87%

Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites

et al. 2020

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“…Other Dps proteins are unable to condense DNA, namely the Dps-1 from Mycobacterium smegmatis, Dps from Mycobacterium abscessus subsp. massiliense and Dps-4 and Dps-5 from the cyanobacterium Nostoc punctiforme (Ceci et al 2007;Moparthi et al 2019;de Alcântara et al 2020). This behavior was attributed to the presence of 4 negatively charged amino acid residues in the C-terminal extension that would compensate (or partly compensate) the 5 positively charged ones.…”

Section: Dna Bindingmentioning

confidence: 99%

Dps–DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration

et al. 2021

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DNA-binding proteins from starved cells (Dps) are members of the ferritin family of proteins found in prokaryotes, with hollow rounded cube-like structures, composed of twelve equal subunits. These protein nanocages are bifunctional enzymes that protect the cell from the harmful reaction of iron and peroxide (Fenton reaction), thus preventing DNA damage by oxidative stress. Ferrous ions are oxidized at specific iron binding sites in the presence of the oxidant and stored in its cavity that can accommodate up to ca. 500 iron atoms. DNA binding properties of Dps are associated with the N-terminal, positive charge rich, extensions that can promote DNA binding and condensation, apparently by a cooperative binding mechanism. Here, we describe the binding and protection activities of Marinobacter hydrocarbonoclasticus Dps using Electrophoretic Mobility Shift Essays (EMSA), and Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. While no DNA condensation was observed in the tested conditions, it was possible to determine a Dps-DNA complex formation with an apparent dissociation constant of 5.9 ± 1.0 µM and a Hill coefficient of 1.2 ± 0.1. This interaction is suppressed by the inclusion of a single negative charge in the N-terminal region by point mutation. In Dps proteins containing a ferric mineral core (above 96 Fe/protein) DNA binding was impaired. SRCD data clearly showed that no significant modification existed either in secondary structure or protein stability of WT, Q14E variant and core containing proteins. It was, however, interesting to note that, in our experimental conditions, thermal denaturation induced protein aggregation that caused artifacts in thermal denaturation curves, which were dependent on radiation flux and vertical arrangement of the CD cell.

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“…31 Ferredoxins are also thought to play a role in iron release of N. punctiforme Dps. 32 Another mode of storage is using encapsulins, which are large macromolecular assemblies similar to viral capsids, widespread in bacteria and archaea. Encapsulins as their name suggests can encapsulate proteins targeted to the capsid via short C-terminal signal sequences present on the cargo proteins.…”

Section: Oxidative Stress and Iron Homeostasismentioning

confidence: 99%

“…In bacterioferritins from P. aeruginosa , a bacterioferritin-associated ferredoxin (Bfd) promotes mobilization of stored iron by binding to BfrB . Ferredoxins are also thought to play a role in iron release of N. punctiforme Dps …”

Section: Oxidative Stress and Iron Homeostasismentioning

confidence: 99%

Dps Functions as a Key Player in Bacterial Iron Homeostasis

Williams,

Chatterji

2023

ACS Omega

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Iron plays a vital role in the maintenance of life, being central to various cellular processes, from respiration to gene regulation. It is essential for iron to be stored in a nontoxic and readily available form. D NA b inding p roteins under s tarvation (Dps) belong to the ferritin family of iron storage proteins and are adept at storing iron in their hollow protein shells. Existing solely in prokaryotes, these proteins have the additional functions of DNA binding and protection from oxidative stress. Iron storage proteins play a functional role in storage, release, and transfer of iron and therefore are central to the optimal functioning of iron homeostasis. Here we review the multifarious properties of Dps through relevant biochemical and structural studies with a focus on iron storage and ferroxidation. We also examine the role of Dps as a possible candidate as an iron donor to iron–sulfur (Fe–S) clusters, which are ubiquitous to many biological processes.

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Structural diffusion properties of two atypical Dps from the cyanobacterium Nostoc punctiforme disclose interactions with ferredoxins and DNA

Cited by 9 publications

References 68 publications

Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites

Biochemical and structural characterization of a thermostable Dps protein with His‐type ferroxidase centers and outer metal‐binding sites

Dps–DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration

Dps Functions as a Key Player in Bacterial Iron Homeostasis

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