DNA Topoisomerases: Enzymes That Control DNA Conformation

Vosberg, Hans−Peter

doi:10.1007/978-3-642-70227-3_2

Cited by 234 publications

(172 citation statements)

References 396 publications

(408 reference statements)

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“…4, lane f), and the relative copy numbers of the plasmids (qualitative estimates based on Figs. [3][4][5] and data hot shown) exhibit no obvious correlation with plasmid DNA supercoiling.…”

Section: Discussionmentioning

confidence: 81%

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Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling.

Pruss¹,

Drlica²

1986

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

172

127

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“…4, lane f), and the relative copy numbers of the plasmids (qualitative estimates based on Figs. [3][4][5] and data hot shown) exhibit no obvious correlation with plasmid DNA supercoiling.…”

Section: Discussionmentioning

confidence: 81%

“…[3][4][5]. It is important, therefore, to understand the interactions that regulate the level of supercoiling and to learn, in molecular terms, what occurs when the normal controls are perturbed or absent.…”

mentioning

confidence: 99%

Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling.

Pruss¹,

Drlica²

1986

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

172

127

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“…DNA topoisomerase II (EC 5.99.1.3; topo II) is an important nuclear scaffold protein implicated in key biological processes including DNA replication and chromosome segregation [1][2][3]. The enzyme is a homodimer that acts to pass a duplex DNA segment through a transient enzyme-bridged double strand break in DNA [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…The enzyme is a homodimer that acts to pass a duplex DNA segment through a transient enzyme-bridged double strand break in DNA [3,4]. Several clinically useful anticancer agents, e.g.…”

Section: Introductionmentioning

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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“…The DNA topoisomerases are a group of enzymes with the ability to interconvert topological isomers of DNA by breaking and resealing phosphodiester bonds (for recent reviews see Liu 1984 ;Vosberg 1985 ;Wang 1985). Type I topoisomerase, first described in prokaryotes by Wang (1971) and in eukaryotes by Champoux and Dulbecco (1972) and later characterized by Keller (1975a, b), change the linking number in steps of one.…”

Section: Introductionmentioning

confidence: 99%

Association of DNA topoisomerase I and RNA polymerase I: a possible role for topoisomerase I in ribosomal gene transcription

et al. 1988

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Abstract. RNA polymerase I preparations purified from a rat hepatoma contained DNA topoisomerase activity. The DNA topoisomerase associated with the polymerase had an Mr of 110000, required Mg2+ but not ATP, and was recognized by anti-topoisomerase I antibodies. When added to RNA polymerase I preparations containing topoisomerase activity, anti-topoisomerase I antibodies were able to inhibit the DNA relaxing activity of the preparation as well as RNA synthesis in vitro. RNA polymerase II prepared by analogous procedures did not contain topoisomerase activity and was not recognized by the antibodies. The topoisomerase I: polymerase I complex was reversibly dissociated by column chromatography on Sephacryl S200 in the presence of 0.25 M (NH 4 hS04. Topoisomerase I was immunolocalized in the transcriptionally active ribosomal gene complex containing RNA polymerase I in situ. These data indicate that topoisomerase I and RNA polymerase I are tightly complexed both in vivo and in vitro, and suggest a role for DNA topoisomerase I in the transcription of ribosomal genes.

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DNA Topoisomerases: Enzymes That Control DNA Conformation

Cited by 234 publications

References 396 publications

Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling.

Topoisomerase I mutants: the gene on pBR322 that encodes resistance to tetracycline affects plasmid DNA supercoiling.

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

Association of DNA topoisomerase I and RNA polymerase I: a possible role for topoisomerase I in ribosomal gene transcription

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