Dps protein is related to resistance of Mycobacterium abscessus subsp. massiliense against stressful conditions

Alcântara, Nayra Rodrigues de; Oliveira, Fábio Muniz de; Garcia, Wânius; Santos, Otávio Augusto Leitão dos; Junqueira-Kipnis, Ana Paula; Kipnis, André

doi:10.1007/s00253-020-10586-z

Cited by 10 publications

(8 citation statements)

References 66 publications

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“…The FA1654 protein is predicted to have an iron binding domain and thus is considered to be a putative DPS protein. DPS proteins are associated with the protection of DNA from Fenton reaction‐mediated oxidative stress (Antipov et al., 2017 ; Bellapadrona et al., 2010 ) via DNA binding and/or iron binding (Antipov et al., 2017 ; de Alcântara et al., 2020 ; Tseng et al., 2019 ). Our studies have indicated that FA1654 can bind iron in vitro.…”

Section: Discussionmentioning

confidence: 99%

Characterization of FA1654: A putative DPS protein in Filifactor alocis

Mangar

Mishra

Yang

et al. 2022

Molecular Oral Microbiology

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The survival/adaptation of Filifactor alocis, a fastidious Gram‐positive asaccharolytic anaerobe, to the inflammatory environment of the periodontal pocket requires an ability to overcome oxidative stress. Moreover, its pathogenic characteristics are highlighted by its capacity to survive in the oxidative‐stress microenvironment of the periodontal pocket and a likely ability to modulate the microbial community dynamics. There is still a significant gap in our understanding of its mechanism of oxidative stress resistance and its impact on the virulence and pathogenicity of the microbial biofilm. Coinfection of epithelial cells with F. alocis and Porphyromonas gingivalis resulted in the upregulation of several genes, including HMPREF0389_01654 (FA1654). Bioinformatics analysis indicates that FA1654 has a “di‐iron binding domain” and could function as a DNA starvation and stationary phase protection (DPS) protein. We have further characterized the FA1654 protein to determine its role in oxidative stress resistance in F. alocis. In the presence of hydrogen peroxide‐induced oxidative stress, there was an ∼1.3 fold upregulation of the FA1654 gene in F. alocis. Incubation of the purified FA1654 protein with DNA in the presence of hydrogen peroxide and iron resulted in the protection of the DNA from Fenton‐mediated degradation. Circular dichroism and differential scanning fluorimetry studies have documented the intrinsic ability of rFA1654 protein to bind iron; however, the rFA1654 protein is missing the intrinsic ability to reduce hydrogen peroxide. Collectively, the data may suggest that FA1654 in F. alocis is involved in oxidative stress resistance via an ability to protect against Fenton‐mediated oxidative stress‐induced damage.

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Section: Discussionmentioning

confidence: 99%

Characterization of FA1654: A putative DPS protein in Filifactor alocis

Mangar

Mishra

Yang

et al. 2022

Molecular Oral Microbiology

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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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“…A bile inducible operon that confers bile tolerance in L. acidophilus NCFM (LBA1425 to LBA1432 [36]) was also present in both CUL21 and CUL60. The genomes of both CUL21 and CUL60 encoded for Dps proteins that are stress regulating proteins implicated in the protection of DNA under a wide variety of conditions (including osmotic, heat [37,38] and oxidative stress [39]). These proteins appear poorly studied in lactobacilli (not at all in L. acidophilus), but have been shown to be upregulated in Lactobacillus plantarum in the presence of bile [40].…”

Section: Survival Colonisation and Persistence Of Lab4 Within The Gastrointestinal Tractmentioning

confidence: 99%