Abstract:
:Camptothecin (CPT), a plant alkaloid with antitumor activity, is a specific inhibitor of eukaryotic DNA topoisomerase I. We have previously isolated and characterized a CPT-resistant topoisomerase I isolated from a CPT-resistant human leukemia cell line, CPT-K5. cDNA clones of topoisomerase I were isolated from the CPT-resistant and the parental CPT-sensitive cell lines, respectively. Sequencing of the clones identified two mutations in the cDNA isolated from the resistant cells, which cause amino acid changes from aspartic acid to glycine at residues 533 and 583 of the parental topoisomerase I. When the CPT-K5 topoisomerase I was expressed in E. coli as a fusion protein with Staphylococcal Protein A fragment, the activity was resistant to CPT at a dose level up to 125 microM, whereas the parental fusion protein was sensitive to CPT as low as 1 microM. The resistance index (greater than 125) of the CPT-K5 fusion topoisomerase I is similar to that of the native CPT-K5 topoisomerase I. These results indicate that either or both of the two amino acid changes identified in the mutant enzyme is responsible for the resistance to CPT.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Tamura H,Kohchi C,Yamada R,Ikeda T,Koiwai O,Patterson E,Keene JD,Okada K,Kjeldsen E,Nishikawa Kdoi
10.1093/nar/19.1.69subject
Has Abstract,Author List Incompletepub_date
1991-01-11 00:00:00pages
69-75issue
1eissn
0305-1048issn
1362-4962journal_volume
19pub_type
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