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Biochem Biophys Res Commun. 2006 Apr 7;342(2):596-604. Epub 2006 Feb 9.

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

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1
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.

Abstract

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.

PMID:
16488395
DOI:
10.1016/j.bbrc.2006.02.006
[Indexed for MEDLINE]
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