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J. Biol. Chem., Vol. 269, Issue 4, 2433-2439, Jan, 1994
E Rubin, P Pantazis, A Bharti, D Toppmeyer, B Giovanella and D Kufe
Human U-937 myeloid leukemia cells were selected for resistance to
increasing concentrations of the camptothecin derivative, 9-nitro-
20(S)camptothecin (9-NC). The isolated single cell clone, designated U-
937/CR, was approximately 20-fold resistant to 9-NC. Analysis of
topoisomerase I (topo I) gene expression in U-937/CR cells demonstrated
similar mRNA levels as compared with U-937 cells. Immunoblotting with an
anti-topo I serum revealed reactive proteins at 100, 75, and 67 kDa which
were expressed at the same level in the parental and 9-NC- resistant
clones. These cell lines also demonstrated similar levels of topo I
catalytic activity as determined by assaying nuclear extracts for
relaxation of supercoiled plasmid DNA. In contrast, catalytic assays
performed in the presence of 9-NC demonstrated that topo I activity from
U-937/CR cells was approximately 10-fold more resistant than that from
U-937 cells. Nucleotide sequencing of topo I cDNAs revealed the
substitution of phenylalanine (TTC) at residue 361 in U- 937 cells with
serine (TCC) in the 9-NC-resistant clone. Expression and partial
purification of the mutant topo I protein in Escherichia coli demonstrated
resistance of this enzyme to 9-NC in catalytic assays. Taken together,
these findings identify a novel mutation in topo I which confers resistance
to 9-NC and support the involvement of this region in the interaction
between topo I and 9-NC.
Identification of a mutant human topoisomerase I with intact catalytic activity and resistance to 9-nitro-camptothecin
Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
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