The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II
- University of Liverpool, School of Clinical Sciences, Division of Gastroenterology, Henry Wellcome Laboratory of Molecular and Cellular Gastroenterology, Crown Street, Liverpool L69 3BX (United Kingdom)
- Compton Paddock Laboratories, Frilsham Home Farm Business Unit, Yattendon, Thatcham RG 18 0XT (United Kingdom)
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.
- OSTI ID:
- 20798883
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 342, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2006.02.006; PII: S0006-291X(06)00289-0; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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