Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal features
A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of 60 and 47 kDa. It has a Stokes radius of 69 A and has a sedimentation coefficient of 7.8 S which gives a calculated native molecular mass of...
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| Published in | The Journal of biological chemistry Vol. 269; no. 44; pp. 27663 - 27669 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
04.11.1994
American Society for Biochemistry and Molecular Biology |
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| Abstract | A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of 60 and 47 kDa. It has a Stokes radius of 69 A and has a sedimentation coefficient of 7.8 S which gives a calculated native molecular mass of approximately 230 kDa, indicating a heterotetrameric structure. This enzyme is ATP and Mg2+ dependent and can relax both negatively and positively supercoiled DNA, but presents no supercoiling activity. The S. shibatae DNA topoisomerase II is more efficient in decatenation than in relaxation. The optimal temperature for the enzymatic activity is approximately 80 degrees C. This archaeal enzyme is not inhibited by the gyrase inhibitor novobiocin but is sensitive to several inhibitors of eucaryotic DNA topoisomerases of type II such as amsacrines, ellipticine, and the quinolone CP-115,953. Like all prokaryotic DNA topoisomerase II, the S. shibatae DNA topoisomerase II is a heterotetramer but the absence of supercoiling activity, the strong decatenase activity, and the pattern of antibiotic sensitivity of the S. shibatae DNA topoisomerase II is reminiscent of eucaryotic enzymes. |
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| AbstractList | A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of 60 and 47 kDa. It has a Stokes radius of 69 angstrom and has a sedimentation coefficient of 7.8 S which gives a calculated native molecular mass of approximately 230 kDa, indicating a heterotetrameric structure. This enzyme is ATP and Mg super(2+) dependent and can relax both negatively and positively supercoiled DNA, but presents no supercoiling activity. The S. shibatae DNA topoisomerase II is more efficient in decatenation than in relaxation. The optimal temperature for the enzymatic activity is similar to 80 degree C. This archaeal enzyme is not inhibited by the gyrase inhibitor novobiocin but is sensitive to several inhibitors of eucaryotic DNA topoisomerases of type II such as amsacrines, ellipticine, and the quinolone CP-115,953. Like all prokaryotic DNA topoisomerase II, the S. shibatae DNA topoisomerase II is a heterotetramer but the absence of supercoiling activity, the strong decatenase activity, and the pattern of antibiotic sensitivity of the S. shibatae DNA topoisomerase II is reminiscent of eucaryotic enzymes. A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of 60 and 47 kDa. It has a Stokes radius of 69 A and has a sedimentation coefficient of 7.8 S which gives a calculated native molecular mass of approximately 230 kDa, indicating a heterotetrameric structure. This enzyme is ATP and Mg2+ dependent and can relax both negatively and positively supercoiled DNA, but presents no supercoiling activity. The S. shibatae DNA topoisomerase II is more efficient in decatenation than in relaxation. The optimal temperature for the enzymatic activity is approximately 80 degrees C. This archaeal enzyme is not inhibited by the gyrase inhibitor novobiocin but is sensitive to several inhibitors of eucaryotic DNA topoisomerases of type II such as amsacrines, ellipticine, and the quinolone CP-115,953. Like all prokaryotic DNA topoisomerase II, the S. shibatae DNA topoisomerase II is a heterotetramer but the absence of supercoiling activity, the strong decatenase activity, and the pattern of antibiotic sensitivity of the S. shibatae DNA topoisomerase II is reminiscent of eucaryotic enzymes. A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of 60 and 47 kDa. It has a Stokes radius of 69 A and has a sedimentation coefficient of 7.8 S which gives a calculated native molecular mass of approximately 230 kDa, indicating a heterotetrameric structure. This enzyme is ATP and Mg2+ dependent and can relax both negatively and positively supercoiled DNA, but presents no supercoiling activity. The S. shibatae DNA topoisomerase II is more efficient in decatenation than in relaxation. The optimal temperature for the enzymatic activity is approximately 80 degrees C. This archaeal enzyme is not inhibited by the gyrase inhibitor novobiocin but is sensitive to several inhibitors of eucaryotic DNA topoisomerases of type II such as amsacrines, ellipticine, and the quinolone CP-115,953. Like all prokaryotic DNA topoisomerase II, the S. shibatae DNA topoisomerase II is a heterotetramer but the absence of supercoiling activity, the strong decatenase activity, and the pattern of antibiotic sensitivity of the S. shibatae DNA topoisomerase II is reminiscent of eucaryotic enzymes. |
| Author | Forterre, P Gadelle, D Bergerat, A |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/7961685$$D View this record in MEDLINE/PubMed |
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| Snippet | A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of... A type II DNA topoisomerase has been purified to homogeneity from the hyperthermophilic archaeon Sulfolobus shibatae. The enzyme is composed of two subunits of... |
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| SubjectTerms | DNA Topoisomerases, Type II - chemistry DNA Topoisomerases, Type II - isolation & purification DNA Topoisomerases, Type II - metabolism Hot Temperature Molecular Weight Protein Conformation Protein Denaturation Substrate Specificity Sulfolobus - enzymology Sulfolobus shibatae Topoisomerase II Inhibitors |
| Title | Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal features |
| URI | https://dx.doi.org/10.1016/S0021-9258(18)47037-8 http://www.jbc.org/content/269/44/27663.abstract https://www.ncbi.nlm.nih.gov/pubmed/7961685 https://search.proquest.com/docview/16628378 https://search.proquest.com/docview/76817046 |
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