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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2000-12-29
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pubmed:abstractText |
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 Deltansr1 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, Deltansr1 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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amsacrine,
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Camptothecin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NSR1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Topoisomerase I Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Topoisomerase II Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36181-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10967121-Amsacrine,
pubmed-meshheading:10967121-Antineoplastic Agents,
pubmed-meshheading:10967121-Camptothecin,
pubmed-meshheading:10967121-Cell Division,
pubmed-meshheading:10967121-DNA Topoisomerases, Type I,
pubmed-meshheading:10967121-DNA Topoisomerases, Type II,
pubmed-meshheading:10967121-Drug Resistance, Microbial,
pubmed-meshheading:10967121-Fungal Proteins,
pubmed-meshheading:10967121-Humans,
pubmed-meshheading:10967121-Microbial Sensitivity Tests,
pubmed-meshheading:10967121-Microscopy, Fluorescence,
pubmed-meshheading:10967121-Mutation,
pubmed-meshheading:10967121-Nuclear Proteins,
pubmed-meshheading:10967121-Protein Binding,
pubmed-meshheading:10967121-Protein Structure, Tertiary,
pubmed-meshheading:10967121-Protein Transport,
pubmed-meshheading:10967121-RNA-Binding Proteins,
pubmed-meshheading:10967121-Recombinant Fusion Proteins,
pubmed-meshheading:10967121-Saccharomyces cerevisiae,
pubmed-meshheading:10967121-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10967121-Subcellular Fractions,
pubmed-meshheading:10967121-Topoisomerase I Inhibitors,
pubmed-meshheading:10967121-Topoisomerase II Inhibitors,
pubmed-meshheading:10967121-Transformation, Genetic
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pubmed:year |
2000
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pubmed:articleTitle |
Role for nucleolin/Nsr1 in the cellular localization of topoisomerase I.
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pubmed:affiliation |
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, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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