DNA repair in hyperthermophilic and hyperradioresistant microorganisms

Ishino, Yuji; Narumi, Issay

doi:10.1016/j.mib.2015.05.010

Cited by 41 publications

(31 citation statements)

References 83 publications

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“…It has been thought that organisms in extreme environments have evolved efficient DNA repair systems to thrive where DNA damage is accelerated. 17,18) However, EndoQ was not found in the phyla, Aquificae, Thermotogae, and Deinococcus-Thermus, including the thermophilic organisms. These bacteria may acquire a pathway different from EndoQ-mediated repair to eliminate base deamination at high temperature environment.…”

Section: Discussionmentioning

confidence: 99%

A functional endonuclease Q exists in the bacterial domain: identification and characterization of endonuclease Q from Bacillus pumilus

Shiraishi

Ishino

Cann

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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DNA base deamination occurs spontaneously under physiological conditions and is promoted by high temperature. Therefore, hyperthermophiles are expected to have efficient repair systems of the deaminated bases in their genomes. Endonuclease Q (EndoQ) was originally identified from the hyperthermophlic archaeon, Pyrococcus furiosus, as a hypoxanthine-specific endonuclease recently. Further biochemical analyses revealed that EndoQ also recognizes uracil, xanthine, and the AP site in DNA, and is probably involved in a specific repair process for damaged bases. Initial phylogenetic analysis showed that an EndoQ homolog is found only in the Thermococcales and some of the methanogens in Archaea, and is not present in most members of the domains Bacteria and Eukarya. A better understanding of the distribution of the EndoQ-mediated repair system is, therefore, of evolutionary interest. We showed here that an EndoQ-like polypeptide from Bacillus pumilus, belonging to the bacterial domain, is functional and has similar properties with the archaeal EndoQs.

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Section: Discussionmentioning

confidence: 99%

A functional endonuclease Q exists in the bacterial domain: identification and characterization of endonuclease Q from Bacillus pumilus

Shiraishi

Ishino

Cann

et al. 2017

Bioscience, Biotechnology, and Biochemistry

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“…In spite of its preferred growth temperature of 72°C (Svetlichny and Svetlichnaya, 1988), D. turdigum has an extremely low (33.96 mol%) G+C content, which seems counterintuitive to genome stability and repair (Ishino and Narumi, 2015). Dtur does possess a reverse gyrase (Dtur_0014), a hallmark enzyme that is systematically present in all hyperthermophiles (Brochier-Armanet and Forterre, 2007), which introduces positive supercoils in DNA and thereby protects it from unwinding.…”

Section: Resultsmentioning

confidence: 99%

The Complete Genome Sequence of Hyperthermophile Dictyoglomus turgidum DSM 6724™ Reveals a Specialized Carbohydrate Fermentor

et al. 2016

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Here we report the complete genome sequence of the chemoorganotrophic, extremely thermophilic bacterium, Dictyoglomus turgidum, which is a Gram negative, strictly anaerobic bacterium. D. turgidum and D. thermophilum together form the Dictyoglomi phylum. The two Dictyoglomus genomes are highly syntenic, and both are distantly related to Caldicellulosiruptor spp. D. turgidum is able to grow on a wide variety of polysaccharide substrates due to significant genomic commitment to glycosyl hydrolases, 16 of which were cloned and expressed in our study. The GH5, GH10, and GH42 enzymes characterized in this study suggest that D. turgidum can utilize most plant-based polysaccharides except crystalline cellulose. The DNA polymerase I enzyme was also expressed and characterized. The pure enzyme showed improved amplification of long PCR targets compared to Taq polymerase. The genome contains a full complement of DNA modifying enzymes, and an unusually high copy number (4) of a new, ancestral family of polB type nucleotidyltransferases designated as MNT (minimal nucleotidyltransferases). Considering its optimal growth at 72°C, D. turgidum has an anomalously low G+C content of 39.9% that may account for the presence of reverse gyrase, usually associated with hyperthermophiles.

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“…Members of the genus Deinococcus are the best known as radioresistant bacteria, and more than 50 Deinococcus species have been isolated from various environments (http://www.bacterio.net/deinococcus.html). Radioresistance in Deinococcus species is attributed to their highly proficient DNA repair capacity (1–4). Deinococcus grandis was initially isolated as a Gram-negative, red-pigmented, radioresistant, rod-shaped bacterium from freshwater fish and named Deinobacter grandis (5).…”

Section: Genome Announcementmentioning

confidence: 99%

“…), which are involved in the unique radiation/desiccation response system in D. radiodurans (4). D. grandis seems to employ the same radioresistance mechanisms as D. radiodurans .…”

Section: Genome Announcementmentioning

confidence: 99%

Draft Genome Sequence of the Radioresistant Bacterium Deinococcus grandis, Isolated from Freshwater Fish in Japan

et al. 2016

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DNA repair in hyperthermophilic and hyperradioresistant microorganisms

Cited by 41 publications

References 83 publications

A functional endonuclease Q exists in the bacterial domain: identification and characterization of endonuclease Q from Bacillus pumilus

A functional endonuclease Q exists in the bacterial domain: identification and characterization of endonuclease Q from Bacillus pumilus

The Complete Genome Sequence of Hyperthermophile Dictyoglomus turgidum DSM 6724™ Reveals a Specialized Carbohydrate Fermentor

Draft Genome Sequence of the Radioresistant Bacterium Deinococcus grandis, Isolated from Freshwater Fish in Japan

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