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Deinococcus radiodurans

ABSTRACT: Radiation-resistant bacterium

PROVIDER: PRJNA35079 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	SRR14698434_1.fastq.gz	Fastqsanger.gz
	SRR14698434_2.fastq.gz	Fastqsanger.gz
	SRR14698435_1.fastq.gz	Fastqsanger.gz
	SRR14698435_2.fastq.gz	Fastqsanger.gz

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Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 strain:R1

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Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 strain:R1

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Deinococcus radiodurans R1: wildtype strains vs. oxyR disruption strains

Project description:In Deinococcus radiodurans, a previously unreported special characteristic of DrOxyR (DR0615) is found with only one conserved cysteine. dr0615 gene mutant is hypersensitive to H2O2, but a little to ionizing radiation. Site-directed mutagenesis and subsequent in vivo functional analyses revealed that the conserved cysteine (C210) is necessary for sensing H2O2, but its mutation did not alter the binding characteristics of OxyR on DNA. Under oxidant stress, DrOxyR is oxidized to sulfenic acid form, which can be reduced by reducing reagents. In addition, quantitative real-time PCR and global transcription profile results showed that OxyR is not only a transcriptional activator (e.g., katE, drb0125), but also a transcriptional repressor (e.g., dps, mntH). Transcriptional profiling of comparing wildtype strains with oxyR disruption strains under normal growth conditions. Keywords: Genetic modification

2008-02-01 | GSE9636 | GEO

Radiation tolerance mechanism of Deinococcus radiodurans using lable-free proteomics

Project description:Even though these results have shown several key proteins played an import role in radiation tolerance mechanism of DR, they were lack of the deep protein coverage, global protein analysis as well as the dynamic changes of DR, which limits further understanding of biological changes in response to ionizing radiation. To the best of our knowledge, the global and specific radiation tolerance mechanism of DR has not been elucidated yet. Therefore, a label-free quantitative proteomics was applied to conduct a systematic and comprehensive proteomic analysis on DR after 6 kGy γ-irradiation at different time point. Differentially abundant proteins (DAPs) with a fold-change cutoff were reported. These proteins, providing a deep understanding of the molecular response to ionizing radiation.

2022-08-29 | PXD027969 | Pride

Deinococcus radiodurans strain:ATCC 35073

Project description:Deinococcus radiodurans UWO 298 below-background gamma radiation transcriptome

| PRJNA389981 | ENA

Thioredoxin system from Deinococcus radiodurans.

Project description:This paper describes the cloning, purification, and characterization of thioredoxin (Trx) and thioredoxin reductase (TrxR) and the structure determination of TrxR from the ionizing radiation-tolerant bacterium Deinococcus radiodurans strain R1. The genes from D. radiodurans encoding Trx and TrxR were amplified by PCR, inserted into a pET expression vector, and overexpressed in Escherichia coli. The overexpressed proteins were purified by metal affinity chromatography, and their activity was demonstrated using well-established assays of insulin precipitation (for Trx), 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) reduction, and insulin reduction (for TrxR). In addition, the crystal structure of oxidized TrxR was determined at 1.9-A resolution. The overall structure was found to be very similar to that of E. coli TrxR and homodimeric with both NADPH- and flavin adenine dinucleotide (FAD)-binding domains containing variants of the canonical nucleotide binding fold, the Rossmann fold. The K(m) (5.7 muM) of D. radiodurans TrxR for D. radiodurans Trx was determined and is about twofold higher than that of the E. coli thioredoxin system. However, D. radiodurans TrxR has a much lower affinity for E. coli Trx (K(m), 44.4 muM). Subtle differences in the surface charge and shape of the Trx binding site on TrxR may account for the differences in recognition. Because it has been suggested that TrxR from D. radiodurans may have dual cofactor specificity (can utilize both NADH and NADPH), D. radiodurans TrxR was tested for its ability to utilize NADH as well. Our results show that D. radiodurans TrxR can utilize only NADPH for activity.

| S-EPMC2805324 | biostudies-literature

Transcriptional Analysis of Deinococcus radiodurans for Novel sRNAs expression that are Differentially Expressed under Ionizing Radiation

Project description:In this study, we identified potential sRNA candidates in D. radiodurans by a whole transcriptome deep sequencing analysis, and confirm the expression of 31 sRNAs in D. radiodurans with Northern blotting analysis and RT-PCR. A total of 8 confirmed sRNAs showed differential expression during recovery after acute ionizing radiation (15 kGy).

2015-01-22 | GSE64952 | GEO

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