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An Archaeal NADH Oxidase Causes Damage to Both Proteins and Nucleic Acids under Oxidative Stress
Jia, Baolei,Lee, Sang-Min,Pham, Bang P.,Cho, Yoon-Seung,Yang, Jae-Kyung,Byeon, Hee-Seop,Kim, Jong-Cheol,Cheong, Gang-Won Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.29 No.4
NADH oxidases (NOXs) catalyze the two-electron reduction of oxygen to $H_2O_2$ or four-electron reduction of oxygen to $H_2O$. In this report, we show that an NADH oxidase from Thermococcus profundus (NOXtp) displays two forms: a native dimeric protein under physiological conditions and an oxidized hexameric form under oxidative stress. Native NOXtp displays high NADH oxidase activity, and oxidized NOXtp can accelerate the aggregation of partially unfolded proteins. The aggregates formed by NOXtp have characteristics similar to ${\beta}$-amyloid and Lewy bodies in neuro-degenerative diseases, including an increase of ${\beta}$-sheet content. Oxidized NOXtp can also bind nucleic acids and cause their degradation by oxidizing NADH to produce $H_2O_2$. Furthermore, Escherichia coli cells expressing NOXtp are less viable than cells not expressing NOXtp after treatment with $H_2O_2$. As NOXtp shares similar features with eukaryotic cell death isozymes and life may have originated from hyperthermophiles, we suggest that NOXtp may be an ancestor of cell death proteins.
An Archaeal NADH Oxidase Causes Damage to Both Proteins and Nucleic Acids under Oxidative Stress
Baolei Jia,이상민,Bang P. Pham,조윤승,양재경,변희섭,김종철,정강원 한국분자세포생물학회 2010 Molecules and cells Vol.29 No.4
NADH oxidases (NOXs) catalyze the two-electron reduction of oxygen to H2O2 or four-electron reduction of oxygen to H2O. In this report, we show that an NADH oxidase from Thermococcus profundus (NOXtp) displays two forms: a native dimeric protein under physiological conditions and an oxidized hexameric form under oxidative stress. Native NOXtp displays high NADH oxidase activity, and oxidized NOXtp can accelerate the aggregation of partially unfolded proteins. The aggregates formed by NOXtp have characteristics similar to β-amyloid and Lewy bodies in neurodegenerative diseases, including an increase of β-sheet content. Oxidized NOXtp can also bind nucleic acids and cause their degradation by oxidizing NADH to produce H2O2. Furthermore, Escherichia coli cells expressing NOXtp are less viable than cells not expressing NOXtp after treatment with H2O2. As NOXtp shares similar features with eukaryotic cell death isozymes and life may have originated from hyperthermophiles,we suggest that NOXtp may be an ancestor of cell death proteins.
Oligomeric Structure of the ATP-dependent Protease La (Lon) of Escherichia coli
박성철,Baolei Jia,양재경,Duyet Le Van,Yong Gi Shao,한상우,전영주,정진하,정강원 한국분자세포생물학회 2006 Molecules and cells Vol.21 No.1
Lon, also known as protease La, belongs to a class of ATP-dependent serine protease. It plays an essential role in degradation of abnormal proteins and of certain short-lived regulatory proteins, and is thought to possess a Ser-Lys catalytic dyad. To examine the structural organization of Lon, we performed an electron microscope analysis. The averaged images of Lon with end-on orientation revealed a six-membered, ringshaped structure with a central cavity. The side-on view showed a two-layered structure with an equal distribution of mass across the equatorial plane of the complex. Since a Lon subunit possesses two large regions containing nucleotide binding and proteolytic domains, each layer of the Lon hexamer appears to consist of the side projections of one of the major domains arranged in a ring. Lon showed a strong tendency to form hexamers in the presence of Mg2+, but dissociated into monomers and/or dimers in its absence. Moreover, Mg2+-dependent hexamer formation was independent of ATP. These results indicate that Lon has a hexameric ring-shaped structure with a central cavity, and that the establishment of this configuration requires Mg2+, but not ATP.
Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli.
Park, Seong-Cheol,Jia, Baolei,Yang, Jae-Kyung,Van, Duyet Le,Shao, Yong Gi,Han, Sang Woo,Jeon, Young-Joo,Chung, Chin Ha,Cheong, Gang-Won Korean Society for Molecular Biology 2006 Molecules and cells Vol.21 No.1
<P>Lon, also known as protease La, belongs to a class of ATP-dependent serine protease. It plays an essential role in degradation of abnormal proteins and of certain short-lived regulatory proteins, and is thought to possess a Ser-Lys catalytic dyad. To examine the structural organization of Lon, we performed an electron microscope analysis. The averaged images of Lon with end-on orientation revealed a six-membered, ring-shaped structure with a central cavity. The side-on view showed a two-layered structure with an equal distribution of mass across the equatorial plane of the complex. Since a Lon subunit possesses two large regions containing nucleotide binding and proteolytic domains, each layer of the Lon hexamer appears to consist of the side projections of one of the major domains arranged in a ring. Lon showed a strong tendency to form hexamers in the presence of Mg(2+), but dissociated into monomers and/or dimers in its absence. Moreover, Mg(2+)-dependent hexamer formation was independent of ATP. These results indicate that Lon has a hexameric ring-shaped structure with a central cavity, and that the establishment of this configuration requires Mg(2+), but not ATP.</P>
Pseudogracilibacillus marinus sp. nov., isolated from a biofilm formed in coastal seawater
Verma, Pankaj,Saravanan, Narasingaperumal,Jia, Baolei,Jeon, Che Ok,Dharani, Gopal,Somasundaram, S. T.,Kirubagaran, Ramalingam Microbiology Society 2016 International journal of systematic and evolutiona Vol.66 No.-