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J. Biol. Chem., Vol. 275, Issue 46, 36181-36188, November 17, 2000
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From the Departments of Medicine/Pharmacology, Cancer Institute of
New Jersey/Robert Wood Johnson Medical School-University of Medicine
and Dentistry of New Jersey, New Brunswick, New
Jersey 08901
Nucleolin functions in ribosome biogenesis
and contains an acidic N terminus that binds nuclear
localization sequences. In previous work we showed that human
nucleolin associates with the N-terminal region of human topoisomerase
I (Top1). We have now mapped the topoisomerase I interaction domain of
nucleolin to the N-terminal 225 amino acids. We also show that the
Saccharomyces cerevisiae nucleolin ortholog, Nsr1p,
physically interacts with yeast topoisomerase I, yTop1p. Studies of
isogenic NSR1+ and
Role for Nucleolin/Nsr1 in the Cellular Localization of
Topoisomerase I*
,,
nsr1 strains indicate that NSR1
is important in determining the cellular localization of yTop1p.
Moreover, deletion of NSR1 reduces sensitivity to
camptothecin, an antineoplastic topoisomerase I inhibitor. By contrast,
nsr1 cells are hypersensitive to the topoisomerase II-targeting drug amsacrine. These findings
indicate that nucleolin/Nsr1 is involved in the cellular localization
of Top1 and that this localization may be important in determining sensitivity to drugs that target topoisomerases.
*
This work was supported by United States Public Health
Service Grants CA70981 and GM59170 (to E. H. R.) and GM51402
(to M. R. G.), awarded by the National Cancer Institute.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
To whom correspondence should be addressed. Tel.: 723-235-7955;
Fax: 723-235-7493; E-mail: ehrubin@umdnj.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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