The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II
Topoisomerase II is required for the viability of all eukaryotic cells. It plays important roles in DNA replication, recombination, chromosome segregation, and the maintenance of the nuclear scaffold. Proteins that interact with and regulate this essential enzyme are of great interest. To investigat...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-04, Vol.342 (2), p.596-604 |
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| creator | Barker, Catherine R. Mouchel, Nathalie A.P. Jenkins, John R. |
| description | Topoisomerase II is required for the viability of all eukaryotic cells. It plays important roles in DNA replication, recombination, chromosome segregation, and the maintenance of the nuclear scaffold. Proteins that interact with and regulate this essential enzyme are of great interest. To investigate the role of proteins interacting with the N-terminal domain of the
Saccharomyces cerevisiae topoisomerase II, we used a yeast two-hybrid protein interaction screen. We identified an interaction between arginyl-tRNA-protein transferase (Ate1) and the N-terminal domain of the
S. cerevisiae topoisomerase II, including the potential site of interaction. Ate1 is a component of the N-end rule protein degradation pathway which targets proteins for degradation. We also propose a previously unidentified role for Ate1 in modulating the level of topoisomerase II through the cell cycle. |
| doi_str_mv | 10.1016/j.bbrc.2006.02.006 |
| format | Article |
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Saccharomyces cerevisiae topoisomerase II, we used a yeast two-hybrid protein interaction screen. We identified an interaction between arginyl-tRNA-protein transferase (Ate1) and the N-terminal domain of the
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Saccharomyces cerevisiae topoisomerase II, we used a yeast two-hybrid protein interaction screen. We identified an interaction between arginyl-tRNA-protein transferase (Ate1) and the N-terminal domain of the
S. cerevisiae topoisomerase II, including the potential site of interaction. Ate1 is a component of the N-end rule protein degradation pathway which targets proteins for degradation. 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Saccharomyces cerevisiae topoisomerase II, we used a yeast two-hybrid protein interaction screen. We identified an interaction between arginyl-tRNA-protein transferase (Ate1) and the N-terminal domain of the
S. cerevisiae topoisomerase II, including the potential site of interaction. Ate1 is a component of the N-end rule protein degradation pathway which targets proteins for degradation. We also propose a previously unidentified role for Ate1 in modulating the level of topoisomerase II through the cell cycle.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16488395</pmid><doi>10.1016/j.bbrc.2006.02.006</doi><tpages>9</tpages></addata></record> |
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| subjects | 60 APPLIED LIFE SCIENCES Amino Acid Sequence Aminoacyltransferases - chemistry Aminoacyltransferases - deficiency Aminoacyltransferases - genetics Aminoacyltransferases - physiology Arginyl-tRNA-protein transferase 1 Binding Sites CELL CYCLE Cell Cycle - genetics CHROMOSOMES DNA REPLICATION DNA Topoisomerases, Type II - chemistry DNA Topoisomerases, Type II - physiology ENZYMES Hot Temperature Humans HYBRIDIZATION Molecular Sequence Data SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae Proteins - antagonists & inhibitors Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - physiology Sequence Deletion Topoisomerase II Topoisomerase II Inhibitors Two-Hybrid System Techniques Yeast two-hybrid |
| title | The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II |
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