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 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.
School of Clinical Sciences, Division of Gastroenterology, The University of Liverpool, Henry Wellcome Laboratory of Molecular and Cellular Gastroenterology, Crown Street, Liverpool L69 3BX, UK.
Catherine R
CR
Barker
Nathalie A P
NA
Mouchel
John R
JR
Jenkins
D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000737:chemistry* / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D001665:Binding Sites; D002453:Cell Cycle / Q000235:genetics; D004250:DNA Topoisomerases, Type II / Q000737:chemistry* / Q000502:physiology*; D006358:Hot Temperature; D006801:Humans; D008969:Molecular Sequence Data; D029701:Saccharomyces cerevisiae Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000502:physiology*; D017384:Sequence Deletion; D059005:Topoisomerase II Inhibitors; D020798:Two-Hybrid System Techniques
D029701:Saccharomyces cerevisiae Proteins; D059005:Topoisomerase II Inhibitors; D019881:Aminoacyltransferases; C019727:arginyltransferase; D004250:DNA Topoisomerases, Type II