Covalent DNA binding by vaccinia topoisomerase results in unpairing of the thymine base 5' of the scissile bond Journal Article
| Authors: | Sekiguchi, J.; Shuman, S. |
| Article Title: | Covalent DNA binding by vaccinia topoisomerase results in unpairing of the thymine base 5' of the scissile bond |
| Abstract: | We have used potassium permanganate to probe contacts between vaccinia DNA topoisomerase and thymine residues in its 5'-CCCTT ↓ DNA target site. Two major conclusions emerge from the experiments presented: (1) permanganate oxidation of the +2T base of the scissile strand interferes with topoisomerase binding to DNA, and (ii) the +1T base of the scissile strand becomes unpaired upon formation of the covalent topoisomerase-DNA intermediate. Disruption of T:A base pairing is confined to the +1-position. Covalently bound DNAs that have experienced this structural distortion (such DNAs being marked by oxidation at +1T) are fully capable of being religated. We suggest that a protein-induced DNA conformational change is a component of the strand passage step of the topoisomerase reaction. |
| Keywords: | nonhuman; protein binding; dna; molecular sequence data; escherichia coli; vaccinia virus; base sequence; base pairing; conformational transition; dna binding; hydrolysis; oxidation-reduction; dna cleavage; dna topoisomerase; dna topoisomerases, type i; vaccinia; thymine; covalent bond; molecular probes; permanganate potassium; priority journal; article; potassium permanganate |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 271 |
| Issue: | 32 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1996-08-09 |
| Start Page: | 19436 |
| End Page: | 19442 |
| Language: | English |
| DOI: | 10.1074/jbc.271.32.19436 |
| PUBMED: | 8702632 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
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