Skip Navigation



Nucleic Acids Research Advance Access published online on June 12, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm434
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (3357K) Freely available
Right arrow Screen PDF (370K) Freely available
Right arrowOA All Versions of this Article:
35/12/4076    most recent
gkm434v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Wyles, J. P.
Right arrow Articles by Cole, S. P.C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wyles, J. P.
Right arrow Articles by Cole, S. P.C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Nuclear interactions of topoisomerase II {alpha} and ß with phospholipid scramblase 1

Jessica P. Wyles, Zhongqin Wu, Shelagh E.L. Mirski and Susan P.C. Cole*

Division of Cancer Biology and Genetics, Cancer Research Institute, Queen's University, Kingston, Ontario, Canada K7L 3N6

*To whom correspondence should be addressed. Tel: +1 613 533 2636; Fax: +1 613 533 6830; Email: spc.cole{at}queensu.ca

Received April 3, 2007. Revised May 11, 2007. Accepted May 14, 2007.

DNA topoisomerase (topo) II modulates DNA topology and is essential for cell division. There are two isoforms of topo II ({alpha} and ß) that have limited functional redundancy, although their catalytic mechanisms appear the same. Using their COOH-terminal domains (CTDs) in yeast two-hybrid analysis, we have identified phospholipid scramblase 1 (PLSCR1) as a binding partner of both topo II {alpha} and ß. Although predominantly a plasma membrane protein involved in phosphatidylserine externalization, PLSCR1 can also be imported into the nucleus where it may have a tumour suppressor function. The interactions of PLSCR1 and topo II were confirmed by pull-down assays with topo II {alpha} and ß CTD fusion proteins and endogenous PLSCR1, and by co-immunoprecipitation of endogenous PLSCR1 and topo II {alpha} and ß from HeLa cell nuclear extracts. PLSCR1 also increased the decatenation activity of human topo II{alpha}. A conserved basic sequence in the CTD of topo II{alpha} was identified as being essential for binding to PLSCR1 and binding of the two proteins could be inhibited by a synthetic peptide corresponding to topo II{alpha} amino acids 1430-1441. These studies reveal for the first time a physical and functional interaction between topo II and PLSCR1.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Br. J. Radiol.Home page
J R Jenkins
A proteomic approach to identifying new drug targets (potentiating topoisomerase II poisons)
Br. J. Radiol., October 1, 2008; 81(Special_Issue_1): S69 - S77.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.