Synthesis of superparamagnetic Co–Pt nanoparticle in Pyrococcus furiosus virus-like particle crystal
Makoto TaniguchiAkifumi HigashiuraNaoto KobayashiDaisuke KandaKakeru TagataRyota FukunishiYasunori YoshikawaEmi KuromatsuNoriaki KishidaYoshinori KotaniKentaro ToyokiTetsuya NakamuraRyoichi NakataniAtsushi NakagawaYu Shiratsuchi
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Superparamagnetism
Pyrococcus furiosus
Crystal (programming language)
The hyperthermophilic archaeon Pyrococcus furiosus can utilize different carbohydrates, such as starch, maltose and trehalose. Uptake of α‐glucosides is mediated by two different, binding protein‐dependent, ATP‐binding cassette (ABC)‐type transport systems. The maltose transporter also transports trehalose, whereas the maltodextrin transport system mediates the uptake of maltotriose and higher malto‐oligosaccharides, but not maltose. Both transport systems are induced during growth on their respective substrates.
Pyrococcus furiosus
Maltotriose
Maltose-binding protein
Hyperthermophile
Maltodextrin
Isomaltose
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Pyrococcus furiosus is a hyperthermophilic archaeon that grows optimally at 100 degrees C. It is not conceivable that these organisms could survive with genomic DNA that was subject to thermal destruction, yet the mechanisms protecting the genomes of this and other hyperthermophiles against such destruction are obscure. We have determined the effect of elevated temperatures up to 110 degrees C on the molecular weight of DNA in intact P. furiosus cells, compared with the effect of elevated temperatures on DNA in the mesothermophilic bacterium Escherichia coli. At 100 degrees C, DNA in P. furiosus cells is about 20 times more resistant to thermal breakage than that in E. coli cells, and six times fewer breaks were found in P. furiosus DNA after exposure to 110 degrees C for 30 min than in E. coli DNA at 95 degrees C. Our hypothesis for this remarkable stability of DNA in a hyperthermophile is that this hyperthermophile possesses DNA-binding proteins that protect against hydrolytic damage, as well as other endogenous protective mechanisms and DNA repair enzyme systems.
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Hyperthermophile
Thermostability
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Pyrococcus furiosus harbours several hydrolytic enzyme activities that enable growth on a variety of polymeric substrates like proteins and polysaccharides. Recently, the organism was shown to exhibit an extremely high β-glucosidase activity, apparently involved in hydrolysis of cellobiose. The cytoplasmic enzyme was purified to homogeneity and its properties were compared with those of other glycosidases. This comparison can be summarized as follows: i) the β-glucosidase activity in cell-free extracts is at least 100-fold higher than the P. furiosus α-glucosidase activity; ii) the β-glucosidase comprises 5% of total cell protein as to only 0.3% for the α-glucosidase; iii) with respect to substrate specifity, Km, pI, and pH-optimum the P. furiosus β-glucosidase resembles other β-glucosidases from microorganisms from lower temperature ranges; iv) compared to these β-glucosidases the P. furiosus enzyme exhibits an enhanced general stability; v) a high similarity is observed with a β-galacto/glucosidase from the hyperthermophile Sulfolobus solfataricus. vi) besides intrinsic features of the enzyme, extrinsic organic compounds appear to determine thermostability of the β-glucosidase.
Pyrococcus furiosus
Hyperthermophile
Thermostability
Sulfolobus solfataricus
Glucosidases
Mesophile
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Pyrococcus furiosus
Rubredoxin
Thermostability
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High pressure synthesis is a powerful technique in searching for new materials. Generally speaking, however, it used to be almost impossible to obtain single crystal samples of these high-pressure phases. To be reported here is the single crystal growths of various transition metal oxides by means of flux method based on the synchrotron X-ray powder diffraction studies at high pressures of several GPa. Some results on the structure analysis based on synchrotron X-ray powder diffraction will also be shown.
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We investigated the capacity of the hyperthermophile Pyrococcus furiosus for DNA repair by measuring survival at high levels of 60Co gamma-irradiation. The P. furiosus 2-Mb chromosome was fragmented into pieces ranging from 500 kb to shorter than 30 kb at a dose of 2,500 Gy and was fully restored upon incubation at 95 degrees C. We suggest that recombination repair could be an extremely active repair mechanism in P. furiosus and that it might be an important determinant of survival of hyperthermophiles at high temperatures.
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Hyperthermophile
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The model organism Pyrococcus furiosus has recently been reported to interact with Methanopyrus kandleri in coculture, suggesting a H 2 symbiosis. In the current study we further investigated this hypothesis by growing P. furiosus with four other hyperthermophilic methanogens providing evidence that the organisms did not only exert positive effects ( P. furiosus/ Methanocaldococcus villosus and P. furiosus/ Methanocaldococcus infernus) on each other, but also neutral ( P. furiosus/ Methanocaldococcus jannaschii) and even inhibitory interactions ( P. furiosus/ Methanotorris igneus) were detected suggesting interspecies relationships not only based on H 2 symbiosis. Using various microscopic techniques we further analyzed the coculture with the highest positive interactions ( P. furiosus/ M. villosus) concerning its growth behavior on various surfaces, which turned out to be in stark contrast to the previous reported coculture of P. furiosus/ M. kandleri. This communication provides new insights into possible interactions of extremophilic Archaea in cocultures and again raises the question if and how hyperthermophilic Archaea communicate besides metabolic intermediates like H 2 .
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Hyperthermophile
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Cloning (programming)
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ABSTRACT Pyrococcus furiosus thermostable amylase (TA) is a cyclodextrin (CD)-degrading enzyme with a high preference for CDs over maltooligosaccharides. In this study, we investigated the roles of four residues (His414, Gly415, Met439, and Asp440) in the function of P. furiosus TA by using site-directed mutagenesis and kinetic analysis. A variant form of P. furiosus TA containing two mutations (H414N and G415E) exhibited strongly enhanced α-(1,4)-transglycosylation activity, resulting in the production of a series of maltooligosaccharides that were longer than the initial substrates. In contrast, the variant enzymes with single mutations (H414N or G415E) showed a substrate preference similar to that of the wild-type enzyme. Other mutations (M439W and D440H) reversed the substrate preference of P. furiosus TA from CDs to maltooligosaccharides. Relative substrate preferences for maltoheptaose over β-CD, calculated by comparing k cat / K m ratios, of 1, 8, and 26 for wild-type P. furiosus TA, P. furiosus TA with D440H, and P. furiosus TA with M439W and D440H, respectively, were found. Our results suggest that His414, Gly415, Met439, and Asp440 play important roles in substrate recognition and transglycosylation. Therefore, this study provides information useful in engineering glycoside hydrolase family 13 enzymes.
Pyrococcus furiosus
Rubredoxin
Thermostability
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