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The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II


, : The identification and characterisation of a functional interaction between arginyl-tRNA-protein transferase and topoisomerase II. Biochemical and Biophysical Research Communications 342(2): 596-604

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 Atel in modulating the level of topoisomerase II through the cell cycle. (c) 2006 Elsevier Inc. All rights reserved.

US$19.90

PMID: 16488395

DOI: 10.1016/j.bbrc.2006.02.006


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