Structure of the Drosophila DNA topoisomerase II gene

Wyckoff, Elizabeth E.; Natalie, Donna; Nolan, Justin M.; Lee, Maxwell; Hsieh, Tao-shih

doi:10.1016/0022-2836(89)90361-6

Cited by 149 publications

(41 citation statements)

References 56 publications

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“…In one approach, amino acid sequences deduced from the nucleotide sequences of the TOP2 genes encoding the yeast S. cerevisiae and Drosophila melanogaster enzymes (21,22) were compared, and stretches of identical sequences were identified. One of these, a 7-amino acid stretch, Met-Ile-Met-Thr-Asp-Gln-Asp, appeared to be particularly attractive because of the low degeneracy of the nucleotide sequences encoding it.…”

Section: Resultsmentioning

confidence: 99%

Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22.

Tsai-Pflugfelder

Liu

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

332

179

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Two overlapping cDNA clones encoding human DNA topoisomerase II were identified by two independent methods. In one, a human cDNA library in phage A was screened by hybridization with a mixed oligonucleotide probe encoding a stretch of seven amino acids found in yeast and Drosophila DNA topoisomerase II; in the other, a different human cDNA library in a Agtll expression vector was screened for the expression of antigenic determinants that are recognized by rabbit antibodies specific to human DNA topoisomerase II. The entire coding sequences of the human DNA topoisomerase II gene were determined from these and several additional clones, identified through the use of the cloned human TOP2 gene sequences as probes. Hybridization between the cloned sequences and mRNA and genomic DNA indicates that the human enzyme is encoded by a single-copy gene. The location of the gene was mapped to chromosome 17q21-22 by in situ hybridization of a cloned fragment to metaphase chromosomes and by hybridization analysis with a panel of mouse-human hybrid cell lines, each retaining a subset of human chromosomes.Eukaryotic DNA topoisomerase II is a ubiquitous ATPdependent type II topoisomerase (reviewed in refs. [1][2][3]

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Section: Resultsmentioning

confidence: 99%

Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22.

Tsai-Pflugfelder

Liu

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

332

179

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“…Fig. 6 shows the homology of the topoisomerase II sequence flanking the alteration site in 10 species (36,50). Tamura and Gellert (48) Chemical mismatch cleavage analysis of topoisomerase II for nucleotide base alterations.…”

Section: Discussionmentioning

confidence: 99%

Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic cells selected for resistance to teniposide.

Bugg

Danks

Beck

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

131

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Nuclear extracts from teniposide (VM-26)-resistant sublines of the human leukemic cell line CCRF-CEM have decreased levels ofDNA topoisomerase Il catalytic activity and decreased capacity to form drug-stabilized covalent protein-DNA complexes. The ATP concentration required for equivalent activity in a DNA-unknotting assay is 2-to 8-fold higher in nuclear extracts from drug-resistant cell lines as compared with the parental line. When adenosine 5' -[B,Yimidoltriphosphate is substituted for ATP in complexformation assays, no significant change is seen with drugsensitive cells, but a 50-65% reduction is seen with VM-26-resistant cells. Collectively, these results indicate that an alteration in ATP binding may be involved in the resistance phenotype. Therefore, we identified regions of the topoisomerase II sequence that conform to previously identified nudeotide-binding sites. Starting with cDNA as the template we determined the sequence of the topoisomerase II mRNA surrounding these sites by sequencing DNA fragments produced by the polymerase chain reaction. In the region corresponding to the consensus B ATP-binding sequence described by DNA topoisomerase II is an essential nuclear enzyme that catalyzes the interconversion of topological forms of doublestranded DNA (1-3). This activity is required for DNA replication, recombination, and chromosome segregation (1,4). The cDNA sequence of a topoisomerase II from HeLa cells (5) corresponded to a 174-kDa protein (170-kDa form). A second distinct form of topoisomerase II having an apparent molecular mass of 180 kDa has been identified (6). The 170-kDa form is more sensitive to the topoisomerase II inhibitors teniposide and merbarone than the 180-kDa form and the two forms differ in their cleavage site, thermal stability, and inhibition by A+T-rich oligonucleotides (7). Chung et al. (8) Several classes of antitumor drugs, including the anthracyclines, epipodophyllotoxins, and aminoacridines, inhibit the catalytic activity of topoisomerase 11 (9-14), and both rodent and human cell lines have been selected for resistance to these drugs (15-21). In most cases cells that have been selected for resistance to a single topoisomerase II-inhibiting drug are cross-resistant to drugs of the other classes. This type of multidrug resistance, termed at-MDR, has been associated with an altered topoisomerase II activity (22-25) or a decrease in the amount of the enzyme (26). Previous studies of the human leukemic cell line CCRF-CEM and two VM-26-resistant sublines showed that topoisomerase II in nuclear extracts from resistant cells required a higher concentration of ATP than an equal amount of topoisomerase II from sensitive cells to achieve equivalent P4 DNA unknotting (20,25). Also, only with extracts from the sensitive cells could adenosine 5'-[/3,'y-imido]triphosphate substitute for ATP to increase covalent topoisomerase II-DNA complexes in the presence of VM-26 or 4'-(9-acridinyl)aminomethanesulfon-m-anisidide (m-AMSA). To characterize this altered ATP interaction at th...

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“…1). It is known that HeLa, Drosophila and other eukaryotic topo II cDNA sequences are closely homologous in the N-terminal two thirds of the coding sequence whereas nucleotide sequences for the Cterminal regions are more divergent [11]. These considerations may explain why the different screening approaches yielded topo II-related cDNA clones that align with different ends of the HeLa p170 cDNA sequence.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of a human cDNA clone encoding a novel DNA topoisomerase II homologue from HeLa cells

Austin¹,

Fisher²

1990

FEBS Letters

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We have isolated and sequenced 3 human DNA topoisomerase II (topo II) partial eDNA clones from a HeLa carcinoma cell eDNA library. Two clones were identical to an internal fragment of HeLa topo II eDNA. The third clone, CAA5, had a different and novel sequence which shared significant nucleotide (62%) and predicted peptide (70%) homologies with a region of the HeLa topo II eDNA. Our results suggest that HeLa cells express at least two homologous forms of DNA topoisomerase II. The new HeLa topo II homologne is discussed in relation to topo II isoenzymes recently described in a Burkitt lymphoma and other cell lines.

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Structure of the Drosophila DNA topoisomerase II gene

Cited by 149 publications

References 56 publications

Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22.

Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22.

Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic cells selected for resistance to teniposide.

Isolation and characterization of a human cDNA clone encoding a novel DNA topoisomerase II homologue from HeLa cells

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