Computational Analysis of DNA Gyrase Action
نویسندگان
چکیده
منابع مشابه
Mechanism of action of DNA gyrase
DNA gyrase is a bacterial motor protein in a class known as topoisomerases, which are responsible for controlling the topological properties of DNA (e.g. amount of supercoiling or catenation). Most topoisomerases can relax supercoiled DNA, which is an energetically favourable process. DNA gyrase is unique amongst this class, because it can introduce supercoils as well as remove them. To wind or...
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The F plasmid-carried bacterial toxin, the CcdB protein, is known to act on DNA gyrase in two different ways. CcdB poisons the gyrase-DNA complex, blocking the passage of polymerases and leading to double-strand breakage of the DNA. Alternatively, in cells that overexpress CcdB, the A subunit of DNA gyrase (GyrA) has been found as an inactive complex with CcdB. We have reconstituted the inactiv...
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DNA gyrase and topoisomerase IV control bacterial DNA topology by breaking DNA, passing duplex DNA through the break, and then resealing the break. This process is subject to reversible corruption by fluoroquinolones, antibacterials that form drug-enzyme-DNA complexes in which the DNA is broken. The complexes, called cleaved complexes due to the presence of DNA breaks, have been crystallized an...
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Tuberculosis and other bacterial diseases represent a significant threat to human health. The DNA topoisomerases are excellent targets for chemotherapy, and DNA gyrase in particular is a well-validated target for antibacterial agents. Naphthoquinones (e.g. diospyrin and 7-methyljuglone) have been shown to have therapeutic potential, particularly against Mycobacterium tuberculosis. We have found...
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In previous studies we have shown that oxolinic acid, a specific inhibitor of the A subunit of DNA gyrase, induces DNA cleavage at 100,000-base-pair intervals on the Escherichia coli chromosome. At subsaturating drug concentrations, cleavage is induced at a fraction of these sites and DNA synthesis is partially inhibited. This partial inhibition is surprisingly rapid even when few sites have be...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2004
ISSN: 0006-3495
DOI: 10.1529/biophysj.104.042994