In vitro affinity of Deinococcus radiodurans MutS towards mismatched DNA exceeds that of its orthologues from Escherichia coli and Thermus thermophilus

Banasik, Michał; Stanisławska-Sachadyn, Anna; Hildebrandt, Ewa; Sachadyn, Paweł

doi:10.1016/j.jbiotec.2017.05.010

Cited by 2 publications

(2 citation statements)

References 28 publications

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“…Furthermore, D. radiodurans MutS has higher affinity for mismatched DNA than E. coli MutS (Banasik et al. 2017), and DnaE polymerase of D. radiodurans , but not that of E. coli , features RecA-dependent DNA polymerase activity (Randi et al. 2016).…”

Section: Dna Repair In Deinococcusmentioning

confidence: 99%

Conservation and diversity of radiation and oxidative stress resistance mechanisms inDeinococcusspecies

Lim

Jung

Blanchard

et al. 2018

FEMS Microbiology Reviews

163

140

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Deinococcus bacteria are famous for their extreme resistance to ionising radiation and other DNA damage- and oxidative stress-generating agents. More than a hundred genes have been reported to contribute to resistance to radiation, desiccation and/or oxidative stress in Deinococcus radiodurans. These encode proteins involved in DNA repair, oxidative stress defence, regulation and proteins of yet unknown function or with an extracytoplasmic location. Here, we analysed the conservation of radiation resistance-associated proteins in other radiation-resistant Deinococcus species. Strikingly, homologues of dozens of these proteins are absent in one or more Deinococcus species. For example, only a few Deinococcus-specific proteins and radiation resistance-associated regulatory proteins are present in each Deinococcus, notably the metallopeptidase/repressor pair IrrE/DdrO that controls the radiation/desiccation response regulon. Inversely, some Deinococcus species possess proteins that D. radiodurans lacks, including DNA repair proteins consisting of novel domain combinations, translesion polymerases, additional metalloregulators, redox-sensitive regulator SoxR and manganese-containing catalase. Moreover, the comparisons improved the characterisation of several proteins regarding important conserved residues, cellular location and possible protein–protein interactions. This comprehensive analysis indicates not only conservation but also large diversity in the molecular mechanisms involved in radiation resistance even within the Deinococcus genus.

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Section: Dna Repair In Deinococcusmentioning

confidence: 99%

Conservation and diversity of radiation and oxidative stress resistance mechanisms inDeinococcusspecies

Lim

Jung

Blanchard

et al. 2018

FEMS Microbiology Reviews

163

140

View full text Add to dashboard Cite

show abstract

“…Deinococcus radiodurans can survive in extreme environments and is highly tolerant to abiotic stresses such as ionizing radiation, desiccation and oxidative stress. It is known as “the strongest microbe in the world” and has attracted much attention from scholars [ 8 , 9 , 10 ]. The genome of D. radiodurans was sequenced in 1999, and there are 3187 ORFs (open reading frames) in the whole genome.…”

Section: Introductionmentioning

confidence: 99%

A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance in Deinococcus radiodurans

Gui

Lin

Yan

et al. 2023

IJMS

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Deinococcus radiodurans is a microorganism that can adjust, survive or thrive in hostile conditions and has been described as “the strongest microorganism in the world”. The underlying mechanism behind the exceptional resistance of this robust bacterium still remains unclear. Osmotic stress, caused by abiotic stresses such as desiccation, salt stress, high temperatures and freezing, is one of the main stresses suffered by microorganisms, and it is also the basic response pathway by which organisms cope with environmental stress. In this study, a unique trehalose synthesis-related gene, dogH (Deinococcus radiodurans orphan glycosyl hydrolase-like family 10), which encodes a novel glycoside hydrolase, was excavated using a multi-omics combination method. The content accumulation of trehalose and its precursors under hypertonic conditions was quantified by HPLC-MS. Ours results showed that the dogH gene was strongly induced by sorbitol and desiccation stress in D. radiodurans. DogH glycoside hydrolase hydrolyzes α-1,4-glycosidic bonds by releasing maltose from starch in the regulation of soluble sugars, thereby increasing the concentration of TreS (trehalose synthase) pathway precursors and trehalose biomass. The maltose and alginate content in D. radiodurans amounted to 48 μg mg protein−1 and 45 μg mg protein−1, respectively, which were 9 and 28 times higher than those in E. coli, respectively. The accumulation of greater intracellular concentrations of osmoprotectants may be the true reason for the higher osmotic stress tolerance of D. radiodurans.

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In vitro affinity of Deinococcus radiodurans MutS towards mismatched DNA exceeds that of its orthologues from Escherichia coli and Thermus thermophilus

Cited by 2 publications

References 28 publications

Conservation and diversity of radiation and oxidative stress resistance mechanisms inDeinococcusspecies

Conservation and diversity of radiation and oxidative stress resistance mechanisms inDeinococcusspecies

A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance in Deinococcus radiodurans

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