Unveiling the Role of Dps in the Organization of Mycobacterial Nucleoid

Ghatak, Payel; Karmakar, Kajari; Kasetty, Sanjay; Chatterji, Dipankar

doi:10.1371/journal.pone.0016019

Cited by 26 publications

(22 citation statements)

References 46 publications

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“…9F,G). This type of protein-DNA complex structure was observed in the Dps1 from M. smegmatis [49], and DNA interaction studies of this protein indicate that the interaction is through its C-terminal region [30], which could be similar for DrDps2 which contains one lysine and two arginine residues (Lys204, Arg209, Arg211) in this region.…”

Section: Dna Interactionmentioning

confidence: 65%

Dps from Deinococcus radiodurans: oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage

et al. 2015

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The DNA binding proteins from starved cells from Deinococcus radiodurans, Dps1-DR2263 and Dps2-DRB0092, have a common overall structure of hollow spherical dodecamers. Their involvement in the homeostasis of intracellular metal and DNA protection was addressed. Our results show that DrDps proteins are able to oxidize ferrous to ferric iron by oxygen or hydrogen peroxide. The iron stored inside the hollow sphere cavity is fully released. Furthermore, these proteins are able to store and release manganese, suggesting they can play a role in manganese homeostasis as well. The interaction of DrDps with DNA was also addressed. Even though DrDps1 binds both linear and coiled DNA, DrDps2 preferentially binds to coiled DNA, forming different protein-DNA complexes, as clearly shown by atomic force microscopy. DrDps1 (dimer and dodecamer) and DrDps2 can protect DNA against reactive oxygen species, although the protection occurs at different Fe to protein ratios. The difference between DrDps could be the result of the DrDps1 higher iron oxidation rate in the presence of hydrogen peroxide and its higher affinity to bind DNA than in DrDps2. Using cellular extracts obtained from D. radiodurans cultures, we showed that DrDps1 oligomers observed in in vitro conditions are also present in vivo. This indicates that DrDps1 has a structural dynamic plasticity that allows its oligomeric state to change between dimer, trimer and dodecamer. This in turn suggests the existence of a regulation mechanism that modulates the oligomer equilibrium and is dependent on growth stages and environmental conditions.

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Section: Dna Interactionmentioning

confidence: 65%

Dps from Deinococcus radiodurans: oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage

et al. 2015

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“…The last species harbours a Dps enzyme that lacks the N-terminal elongation but instead shows a positively charged outer molecular surface [23,110,113,[115][116][117][118][119][120][121][122][123]. In contrast with E. coli, the Dps enzyme from M. smegmatis carries a C-terminal extension that is of importance for DNA in vitro [124,125]. Interestingly, in analogy to the N-terminus of E. coli, this extension carries five positively charged residues ( .…”

Section: The Diverse Functions Of Dps Proteins: Peroxidase Reaction Amentioning

confidence: 99%

Dps biomineralizing proteins: multifunctional architects of nature

Zeth

2012

Biochemical Journal

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Dps proteins are the structural relatives of bacterioferritins and ferritins ubiquitously present in the bacterial and archaeal kingdoms. The ball-shaped enzymes play important roles in the detoxification of ROS (reactive oxygen species), in iron scavenging to prevent Fenton reactions and in the mechanical protection of DNA. Detoxification of ROS and iron chaperoning represent the most archetypical functions of dodecameric Dps enzymes. Recent crystallographic studies of these dodecameric complexes have unravelled species-dependent mechanisms of iron uptake into the hollow spheres. Subsequent functions in iron oxidation at ferroxidase centres are highly conserved among bacteria. Final nucleation of iron as iron oxide nanoparticles has been demonstrated to originate at acidic residues located on the inner surface. Some Dps enzymes are also implicated in newly observed catalytic functions related to the formation of molecules playing roles in bacterium–host cell communication. Most recently, Dps complexes are attracting attention in semiconductor science as biomimetic tools for the technical production of the smallest metal-based quantum nanodots used in nanotechnological approaches, such as memory storage or solar cell development.

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“…A limited number of bacteria have multiple Dps, e.g. Bacillus anthracis , Deinococcus radiodurans and Mycobacterium smegmatis (Schwartz et al ., ; Ghatak et al ., ; Reon et al ., ). On the basis of sequenced bacterial genomes (see, i.e.…”

Section: Introductionmentioning

confidence: 98%

Cellular and functional specificity among ferritin‐like proteins in the multicellular cyanobacterium Nostoc punctiforme

Ekman

Sandh

Nenninger

et al. 2013

Environmental Microbiology

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Ferritin-like proteins constitute a remarkably heterogeneous protein family, including ferritins, bacterioferritins and Dps proteins. The genome of the filamentous heterocyst-forming cyanobacterium Nostoc punctiforme encodes five ferritin-like proteins. In the present paper, we report a multidimensional characterization of these proteins. Our phylogenetic and bioinformatics analyses suggest both structural and physiological differences among the ferritin-like proteins. The expression of these five genes responded differently to hydrogen peroxide treatment, with a significantly higher rise in transcript level for Npun_F3730 as compared with the other four genes. A specific role for Npun_F3730 in the cells tolerance against hydrogen peroxide was also supported by the inactivation of Npun_F3730, Npun_R5701 and Npun_R6212; among these, only the ΔNpun_F3730 strain showed an increased sensitivity to hydrogen peroxide compared with wild type. Analysis of promoter-GFP reporter fusions of the ferritin-like genes indicated that Npun_F3730 and Npun_R5701 were expressed in all cell types of a diazotrophic culture, while Npun_F6212 was expressed specifically in heterocysts. Our study provides the first comprehensive analysis combining functional differentiation and cellular specificity within this important group of proteins in a multicellular cyanobacterium.

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Unveiling the Role of Dps in the Organization of Mycobacterial Nucleoid

Cited by 26 publications

References 46 publications

Dps from Deinococcus radiodurans: oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage

Dps from Deinococcus radiodurans: oligomeric forms of Dps1 with distinct cellular functions and Dps2 involved in metal storage

Dps biomineralizing proteins: multifunctional architects of nature

Cellular and functional specificity among ferritin‐like proteins in the multicellular cyanobacterium Nostoc punctiforme

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