Ceci 2011 Extremophiles: Difference between revisions
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{{Publication | {{Publication | ||
|title=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E (2011) The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress. Extremophiles 15: 431- | |title=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E (2011) The characterization of ''Thermotoga maritima'' ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress. Extremophiles 15:431-9. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/21487935 PMID:21487935] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/21487935 PMID: 21487935] | ||
|authors=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E | |authors=Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E | ||
|year=2011 | |year=2011 | ||
|journal=Extremophiles | |journal=Extremophiles | ||
|abstract=Ferritin from the hyperthermophilic anaerobe Thermotoga maritima, a bacterium of ancient phylogenetic origin, is structurally similar to known bacterial and eukaryotic ferritins: 24 identical subunits assemble into a shell having octahedral symmetry and a Mr of about 460 kDa. T. maritima ferritin (TmFtn), purified to homogeneity as a recombinant protein, contains approximately 2-3 iron atoms and can incorporate efficiently up to 3,500 atoms in the form of a ferric oxy-hydroxide mineral at | |abstract=Ferritin from the hyperthermophilic anaerobe ''Thermotoga maritima'', a bacterium of ancient phylogenetic origin, is structurally similar to known bacterial and eukaryotic ferritins: 24 identical subunits assemble into a shell having octahedral symmetry and a Mr of about 460 kDa. ''T. maritima'' ferritin (TmFtn), purified to homogeneity as a recombinant protein, contains approximately 2-3 iron atoms and can incorporate efficiently up to 3,500 atoms in the form of a ferric oxy-hydroxide mineral at 80 ยฐC, the optimal growth temperature of the bacterium. The 24-mer unexpectedly dissociates reversibly into dimers at low ionic strengths. In turn, dimers re-associate into the native 24-mer assembly at high protein concentrations and upon incorporation of iron micelles containing at least 500 Fe(III). TmFtn uses O<sub>2</sub> as efficient iron oxidant. The reaction stoichiometry is 3-4 O<sub>2</sub>:Fe(II) as in all bacterial ferritins. Accordingly no H<sub>2</sub>O<sub>2</sub> is released into solution, a feature reflected in the in vitro ability of TmFtn to reduce significantly iron-mediated oxidative damage to DNA at 80 ยฐC. A similar TmFtn-mediated ROS detoxifying role likely occurs in the bacterium which lacks the SOD/catalase defense systems of the aerobic world. | ||
|keywords= | |keywords=Thermotoga maritima ferritin, Subunit association-dissociation properties, Iron incorporation, DNA protection, ROS detoxification | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Rat, Eubacteria | |||
|preparations=Enzyme | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} |
Latest revision as of 09:46, 9 November 2016
Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E (2011) The characterization of Thermotoga maritima ferritin reveals an unusual subunit dissociation behavior and efficient DNA protection from iron-mediated oxidative stress. Extremophiles 15:431-9. |
Ceci P, Forte E, Di Cecca G, Fornara M, Chiancone E (2011) Extremophiles
Abstract: Ferritin from the hyperthermophilic anaerobe Thermotoga maritima, a bacterium of ancient phylogenetic origin, is structurally similar to known bacterial and eukaryotic ferritins: 24 identical subunits assemble into a shell having octahedral symmetry and a Mr of about 460 kDa. T. maritima ferritin (TmFtn), purified to homogeneity as a recombinant protein, contains approximately 2-3 iron atoms and can incorporate efficiently up to 3,500 atoms in the form of a ferric oxy-hydroxide mineral at 80 ยฐC, the optimal growth temperature of the bacterium. The 24-mer unexpectedly dissociates reversibly into dimers at low ionic strengths. In turn, dimers re-associate into the native 24-mer assembly at high protein concentrations and upon incorporation of iron micelles containing at least 500 Fe(III). TmFtn uses O2 as efficient iron oxidant. The reaction stoichiometry is 3-4 O2:Fe(II) as in all bacterial ferritins. Accordingly no H2O2 is released into solution, a feature reflected in the in vitro ability of TmFtn to reduce significantly iron-mediated oxidative damage to DNA at 80 ยฐC. A similar TmFtn-mediated ROS detoxifying role likely occurs in the bacterium which lacks the SOD/catalase defense systems of the aerobic world. โข Keywords: Thermotoga maritima ferritin, Subunit association-dissociation properties, Iron incorporation, DNA protection, ROS detoxification
Labels:
Organism: Rat, Eubacteria
Preparation: Enzyme
HRR: Oxygraph-2k