Publication Date:
1999-10-16
Description:
Covalent intermediates between topoisomerase I and DNA can become dead-end complexes that lead to cell death. Here, the isolation of the gene for an enzyme that can hydrolyze the bond between this protein and DNA is described. Enzyme-defective mutants of yeast are hypersensitive to treatments that increase the amount of covalent complexes, indicative of enzyme involvement in repair. The gene is conserved in eukaryotes and identifies a family of enzymes that has not been previously recognized. The presence of this gene in humans may have implications for the effectiveness of topoisomerase I poisons, such as the camptothecins, in chemotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pouliot, J J -- Yao, K C -- Robertson, C A -- Nash, H A -- New York, N.Y. -- Science. 1999 Oct 15;286(5439):552-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Mental Health, Building 36, Room 1B08, Bethesda, MD 20892-4034, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10521354" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Camptothecin/pharmacology
;
*DNA Repair
;
DNA Topoisomerases, Type I/genetics/*metabolism
;
DNA, Fungal/*metabolism
;
Expressed Sequence Tags
;
Genes, Fungal
;
Humans
;
Molecular Sequence Data
;
Mutation
;
Phosphoric Diester Hydrolases/chemistry/*genetics/metabolism
;
Saccharomyces cerevisiae/drug effects/enzymology/*genetics
;
Sequence Alignment
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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