SLESAREV, AI and STETTER, KO and LAKE, JA and GELLERT, M and KRAH, R and KOZYAVKIN, SA (1993) DNA TOPOISOMERASE-V IS A RELATIVE OF EUKARYOTIC TOPOISOMERASE-I FROM A HYPERTHERMOPHILIC PROKARYOTE. NATURE, 364 (6439). pp. 735-736. ISSN 0028-0836,
Full text not available from this repository.Abstract
THE DNA topoisomerases are ubiquitous enzymes that fulfil vital roles in the replication, transcription and recombination of DNA by carrying out DNA-strand passage reactions1-7. Here we characterize a prokaryotic counterpart to the eukaryotic topoisomerase I in the hyperthermophilic methanogen Methanopyrus kandleri8-10. The new enzyme, called topoisomerase V, has the following properties in common with eukaryotic topoisomerase I, which distinguish it from all other known prokaryotic topoisomerases: (1) its activity is Mg2+-independent; (2) it relaxes both negatively and positively supercoiled DNA; (3) it makes a covalent complex with the 3' end of the broken DNA strand; and (4) it is recognized by antibody raised against human topoisomerase I. Eukaryotic-like enzymes have been discovered in some hyperthermophilic prokaryotes, namely the eocytes11 and the extremely thermophilic archaebacteria12, and hyperthermophilic homologues of eukaryotic DNA polymerase-a, transcription factor IIB and DNA ligase13-15 have all been reported. Thus our findings support the idea that some essential parts of the eukaryotic transcription-translation and replication machineries were in place before the emergence of eukaryotes, and that the closest living relatives of eukaryotes may be hyperthermophiles.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DESULFUROCOCCUS-AMYLOLYTICUS; METHANOPYRUS-KANDLERI; ARCHAEBACTERIA; 110-DEGREES-C; METHANOGENS; ARCHAEA; GENE; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53825 |
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