Inhibition of postreplication recombinational repair by DNA-Gyrase antagonists in Escherichia coli

Esther Priel

doi:10.1016/0309-1651(84)90116-4

Inhibition of postreplication recombinational repair by DNA-Gyrase antagonists in Escherichia coli

Esther Priel

The Shraga Segal Department of Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

In the present study we investigated the possible involvment of DNA-Gyrase in postreplication repair in E. Coli. It was observed that nalidixic acid and oxolinic acid (which are known-antagonists of DNA - Gyrase) inhibited recombinational repair. These results strongly suggest that the nicking closing activity of DNA - Gyrase is essential for efficient recombinational repair.

Original language	English
Pages (from-to)	773-786
Number of pages	14
Journal	Cell Biology International Reports
Volume	8
Issue number	9
DOIs	https://doi.org/10.1016/0309-1651(84)90116-4
State	Published - 1 Jan 1984

ASJC Scopus subject areas

Cell Biology

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10.1016/0309-1651(84)90116-4

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title = "Inhibition of postreplication recombinational repair by DNA-Gyrase antagonists in Escherichia coli",

abstract = "In the present study we investigated the possible involvment of DNA-Gyrase in postreplication repair in E. Coli. It was observed that nalidixic acid and oxolinic acid (which are known-antagonists of DNA - Gyrase) inhibited recombinational repair. These results strongly suggest that the nicking closing activity of DNA - Gyrase is essential for efficient recombinational repair.",

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AB - In the present study we investigated the possible involvment of DNA-Gyrase in postreplication repair in E. Coli. It was observed that nalidixic acid and oxolinic acid (which are known-antagonists of DNA - Gyrase) inhibited recombinational repair. These results strongly suggest that the nicking closing activity of DNA - Gyrase is essential for efficient recombinational repair.

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Inhibition of postreplication recombinational repair by DNA-Gyrase antagonists in Escherichia coli

Abstract

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