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The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75...
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | European Journal of Biochemistry, 267, 2000, 4, S. 1125-1137 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav |
|---|---|
| author |
Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav |
| spellingShingle |
Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav European Journal of Biochemistry The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C Biochemistry |
| author_sort |
spies, maria |
| spelling |
Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.2000.01108.x <jats:p>The <jats:italic>radA</jats:italic> gene is an archaeal homolog of bacterial <jats:italic>recA</jats:italic> and eukaryotic <jats:italic>RAD51</jats:italic> genes, which are critical components in homologous recombination and recombinational DNA repair. We cloned the <jats:italic>radA</jats:italic> gene from a hyperthermophilic archaeon, <jats:italic>Pyrobaculum islandicum</jats:italic>, overproduced the <jats:italic>radA</jats:italic> gene product in <jats:italic>Escherichia coli</jats:italic> and purified it to homogeneity. The purified <jats:italic>P. islandicum</jats:italic> RadA protein maintained its secondary structure and activities <jats:italic>in vitro</jats:italic> at high temperatures, up to 87 °C. It also showed high stability of 18.3 kcal·mol<jats:sup>−1</jats:sup> (76.5 kJ·mol<jats:sup>−1</jats:sup>) at 25 °C and neutral pH. <jats:italic>P. islandicum</jats:italic> RadA exhibited activities typical of the family of RecA‐like proteins, such as the ability to bind ssDNA, to hydrolyze ATP in a DNA‐dependent manner and to catalyze DNA strand exchange. At 75 °C, all DNAs tested stimulated ATPase activity of the RadA. The protein exhibited a break in the Arrhenius plot of ATP hydrolysis at 75 °C. The cooperativity of ATP hydrolysis and ssDNA‐binding ability of the protein above 75 °C were higher than at lower temperatures, and the activation energy of ATP hydrolysis was lower above this break point temperature. These results suggest that the ssDNA‐dependent ATPase activity of <jats:italic>P. islandicum</jats:italic> RadA displays a temperature‐dependent capacity to exist in two different catalytic modes, with 75 °C being the critical threshold temperature.</jats:p> The RadA protein from a hyperthermophilic archaeon <i>Pyrobaculum islandicum</i> is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C European Journal of Biochemistry |
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Wiley, 2000 |
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European Journal of Biochemistry |
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| title |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_unstemmed |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_full |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_fullStr |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_full_unstemmed |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_short |
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_sort |
the rada protein from a hyperthermophilic archaeon <i>pyrobaculum islandicum</i> is a dna‐dependent atpase that exhibits two disparate catalytic modes, with a transition temperature at 75 °c |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1046/j.1432-1327.2000.01108.x |
| publishDate |
2000 |
| physical |
1125-1137 |
| description |
<jats:p>The <jats:italic>radA</jats:italic> gene is an archaeal homolog of bacterial <jats:italic>recA</jats:italic> and eukaryotic <jats:italic>RAD51</jats:italic> genes, which are critical components in homologous recombination and recombinational DNA repair. We cloned the <jats:italic>radA</jats:italic> gene from a hyperthermophilic archaeon, <jats:italic>Pyrobaculum islandicum</jats:italic>, overproduced the <jats:italic>radA</jats:italic> gene product in <jats:italic>Escherichia coli</jats:italic> and purified it to homogeneity. The purified <jats:italic>P. islandicum</jats:italic> RadA protein maintained its secondary structure and activities <jats:italic>in vitro</jats:italic> at high temperatures, up to 87 °C. It also showed high stability of 18.3 kcal·mol<jats:sup>−1</jats:sup> (76.5 kJ·mol<jats:sup>−1</jats:sup>) at 25 °C and neutral pH. <jats:italic>P. islandicum</jats:italic> RadA exhibited activities typical of the family of RecA‐like proteins, such as the ability to bind ssDNA, to hydrolyze ATP in a DNA‐dependent manner and to catalyze DNA strand exchange. At 75 °C, all DNAs tested stimulated ATPase activity of the RadA. The protein exhibited a break in the Arrhenius plot of ATP hydrolysis at 75 °C. The cooperativity of ATP hydrolysis and ssDNA‐binding ability of the protein above 75 °C were higher than at lower temperatures, and the activation energy of ATP hydrolysis was lower above this break point temperature. These results suggest that the ssDNA‐dependent ATPase activity of <jats:italic>P. islandicum</jats:italic> RadA displays a temperature‐dependent capacity to exist in two different catalytic modes, with 75 °C being the critical threshold temperature.</jats:p> |
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| author | Spies, Maria, Kil, Yuri, Masui, Ryoji, Kato, Ryuichi, Kujo, Chizu, Ohshima, Toshihisa, Kuramitsu, Seiki, Lanzov, Vladislav |
| author_facet | Spies, Maria, Kil, Yuri, Masui, Ryoji, Kato, Ryuichi, Kujo, Chizu, Ohshima, Toshihisa, Kuramitsu, Seiki, Lanzov, Vladislav, Spies, Maria, Kil, Yuri, Masui, Ryoji, Kato, Ryuichi, Kujo, Chizu, Ohshima, Toshihisa, Kuramitsu, Seiki, Lanzov, Vladislav |
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| description | <jats:p>The <jats:italic>radA</jats:italic> gene is an archaeal homolog of bacterial <jats:italic>recA</jats:italic> and eukaryotic <jats:italic>RAD51</jats:italic> genes, which are critical components in homologous recombination and recombinational DNA repair. We cloned the <jats:italic>radA</jats:italic> gene from a hyperthermophilic archaeon, <jats:italic>Pyrobaculum islandicum</jats:italic>, overproduced the <jats:italic>radA</jats:italic> gene product in <jats:italic>Escherichia coli</jats:italic> and purified it to homogeneity. The purified <jats:italic>P. islandicum</jats:italic> RadA protein maintained its secondary structure and activities <jats:italic>in vitro</jats:italic> at high temperatures, up to 87 °C. It also showed high stability of 18.3 kcal·mol<jats:sup>−1</jats:sup> (76.5 kJ·mol<jats:sup>−1</jats:sup>) at 25 °C and neutral pH. <jats:italic>P. islandicum</jats:italic> RadA exhibited activities typical of the family of RecA‐like proteins, such as the ability to bind ssDNA, to hydrolyze ATP in a DNA‐dependent manner and to catalyze DNA strand exchange. At 75 °C, all DNAs tested stimulated ATPase activity of the RadA. The protein exhibited a break in the Arrhenius plot of ATP hydrolysis at 75 °C. The cooperativity of ATP hydrolysis and ssDNA‐binding ability of the protein above 75 °C were higher than at lower temperatures, and the activation energy of ATP hydrolysis was lower above this break point temperature. These results suggest that the ssDNA‐dependent ATPase activity of <jats:italic>P. islandicum</jats:italic> RadA displays a temperature‐dependent capacity to exist in two different catalytic modes, with 75 °C being the critical threshold temperature.</jats:p> |
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| imprint | Wiley, 2000 |
| imprint_str_mv | Wiley, 2000 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
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| spelling | Spies, Maria Kil, Yuri Masui, Ryoji Kato, Ryuichi Kujo, Chizu Ohshima, Toshihisa Kuramitsu, Seiki Lanzov, Vladislav 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.2000.01108.x <jats:p>The <jats:italic>radA</jats:italic> gene is an archaeal homolog of bacterial <jats:italic>recA</jats:italic> and eukaryotic <jats:italic>RAD51</jats:italic> genes, which are critical components in homologous recombination and recombinational DNA repair. We cloned the <jats:italic>radA</jats:italic> gene from a hyperthermophilic archaeon, <jats:italic>Pyrobaculum islandicum</jats:italic>, overproduced the <jats:italic>radA</jats:italic> gene product in <jats:italic>Escherichia coli</jats:italic> and purified it to homogeneity. The purified <jats:italic>P. islandicum</jats:italic> RadA protein maintained its secondary structure and activities <jats:italic>in vitro</jats:italic> at high temperatures, up to 87 °C. It also showed high stability of 18.3 kcal·mol<jats:sup>−1</jats:sup> (76.5 kJ·mol<jats:sup>−1</jats:sup>) at 25 °C and neutral pH. <jats:italic>P. islandicum</jats:italic> RadA exhibited activities typical of the family of RecA‐like proteins, such as the ability to bind ssDNA, to hydrolyze ATP in a DNA‐dependent manner and to catalyze DNA strand exchange. At 75 °C, all DNAs tested stimulated ATPase activity of the RadA. The protein exhibited a break in the Arrhenius plot of ATP hydrolysis at 75 °C. The cooperativity of ATP hydrolysis and ssDNA‐binding ability of the protein above 75 °C were higher than at lower temperatures, and the activation energy of ATP hydrolysis was lower above this break point temperature. These results suggest that the ssDNA‐dependent ATPase activity of <jats:italic>P. islandicum</jats:italic> RadA displays a temperature‐dependent capacity to exist in two different catalytic modes, with 75 °C being the critical threshold temperature.</jats:p> The RadA protein from a hyperthermophilic archaeon <i>Pyrobaculum islandicum</i> is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C European Journal of Biochemistry |
| spellingShingle | Spies, Maria, Kil, Yuri, Masui, Ryoji, Kato, Ryuichi, Kujo, Chizu, Ohshima, Toshihisa, Kuramitsu, Seiki, Lanzov, Vladislav, European Journal of Biochemistry, The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C, Biochemistry |
| title | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_full | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_fullStr | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_full_unstemmed | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_short | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| title_sort | the rada protein from a hyperthermophilic archaeon <i>pyrobaculum islandicum</i> is a dna‐dependent atpase that exhibits two disparate catalytic modes, with a transition temperature at 75 °c |
| title_unstemmed | The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA‐dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75 °C |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1046/j.1432-1327.2000.01108.x |