Dps Functions as a Key Player in Bacterial Iron Homeostasis

Williams, Sunanda Margrett; Chatterji, Dipankar

doi:10.1021/acsomega.3c03277

Cited by 7 publications

(3 citation statements)

References 107 publications

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“…examined so far [ 29 ]. Balancing of Mn/Fe ratio is also effected by maintaining iron homeostasis wherein Dps-like proteins play a crucial role [ 141 ]. These are ferritin family proteins responsible for iron sequestration, ferroxidation and binding to DNA to protect it from oxidative damage [ 100 , 141 ].…”

Section: Resultsmentioning

confidence: 99%

“…Balancing of Mn/Fe ratio is also effected by maintaining iron homeostasis wherein Dps-like proteins play a crucial role [ 141 ]. These are ferritin family proteins responsible for iron sequestration, ferroxidation and binding to DNA to protect it from oxidative damage [ 100 , 141 ]. Bourne out of the genome analysis, VITHBRA024 has two such proteins i.e., Dps and MrgA, while VITHBRA001 has one Dps.…”

Section: Resultsmentioning

confidence: 99%

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Unraveling radiation resistance strategies in two bacterial strains from the high background radiation area of Chavara-Neendakara: A comprehensive whole genome analysis

Pal,

Yuvaraj,

Krishnan

et al. 2024

PLoS ONE

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This paper reports the results of gamma irradiation experiments and whole genome sequencing (WGS) performed on vegetative cells of two radiation resistant bacterial strains, Metabacillus halosaccharovorans (VITHBRA001) and Bacillus paralicheniformis (VITHBRA024) (D10 values 2.32 kGy and 1.42 kGy, respectively), inhabiting the top-ranking high background radiation area (HBRA) of Chavara-Neendakara placer deposit (Kerala, India). The present investigation has been carried out in the context that information on strategies of bacteria having mid-range resistance for gamma radiation is inadequate. WGS, annotation, COG and KEGG analyses and manual curation of genes helped us address the possible pathways involved in the major domains of radiation resistance, involving recombination repair, base excision repair, nucleotide excision repair and mismatch repair, and the antioxidant genes, which the candidate could activate to survive under ionizing radiation. Additionally, with the help of these data, we could compare the candidate strains with that of the extremely radiation resistant model bacterium Deinococccus radiodurans, so as to find the commonalities existing in their strategies of resistance on the one hand, and also the rationale behind the difference in D10, on the other. Genomic analysis of VITHBRA001 and VITHBRA024 has further helped us ascertain the difference in capability of radiation resistance between the two strains. Significantly, the genes such as uvsE (NER), frnE (protein protection), ppk1 and ppx (non-enzymatic metabolite production) and those for carotenoid biosynthesis, are endogenous to VITHBRA001, but absent in VITHBRA024, which could explain the former’s better radiation resistance. Further, this is the first-time study performed on any bacterial population inhabiting an HBRA. This study also brings forward the two species whose radiation resistance has not been reported thus far, and add to the knowledge on radiation resistant capabilities of the phylum Firmicutes which are abundantly observed in extreme environment.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Unraveling radiation resistance strategies in two bacterial strains from the high background radiation area of Chavara-Neendakara: A comprehensive whole genome analysis

Pal,

Yuvaraj,

Krishnan

et al. 2024

PLoS ONE

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“…This storage system prevents the potentially catastrophic consequences of the Fenton reaction and remobilizes the iron to satisfy cellular requirements during starvation. The main bacterial iron storage proteins are bacterial ferritins (Ftns), bacterioferritins (Bfrs), DNA–binding proteins from starved cells (Dps), and encapsulated ferritin-like proteins (FLPs) [ 27 , 28 , 29 , 30 , 31 , 32 ]. This review will focus on the structural and functional characteristics of the encapsulated FLPs.…”

Section: Introductionmentioning

confidence: 99%

Encapsulated Ferritin-like Proteins: A Structural Perspective

Eren,

Watts,

Montecinos

et al. 2024

Biomolecules

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Encapsulins are self–assembling nano–compartments that naturally occur in bacteria and archaea. These nano–compartments encapsulate cargo proteins that bind to the shell’s interior through specific recognition sequences and perform various metabolic processes. Encapsulation enables organisms to perform chemical reactions without exposing the rest of the cell to potentially harmful substances while shielding cargo molecules from degradation and other adverse effects of the surrounding environment. One particular type of cargo protein, the ferritin–like protein (FLP), is the focus of this review. Encapsulated FLPs are members of the ferritin–like protein superfamily, and they play a crucial role in converting ferrous iron (Fe+2) to ferric iron (Fe+3), which is then stored inside the encapsulin in mineralized form. As such, FLPs regulate iron homeostasis and protect organisms against oxidative stress. Recent studies have demonstrated that FLPs have tremendous potential as biosensors and bioreactors because of their ability to catalyze the oxidation of ferrous iron with high specificity and efficiency. Moreover, they have been investigated as potential targets for therapeutic intervention in cancer drug development and bacterial pathogenesis. Further research will likely lead to new insights and applications for these remarkable proteins in biomedicine and biotechnology.

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