YacG from Escherichia coli is a specific endogenous inhibitor of DNA gyrase.
We assign a function for a small protein, YacG encoded by Escherichia coli genome. The NMR structure of YacG shows the presence of an unusual zinc-finger motif. YacG was predicted to be a part of DNA gyrase interactome based on protein-protein interaction network. We demonstrate that YacG inhibits all the catalytic activities of DNA gyrase by preventing its DNA binding. Topoisomerase I and IV activities remain unaltered in the presence of YacG and its action appears to be restricted only to DNA gyrase. The inhibition of the enzyme activity is due to the binding of YacG to carboxyl terminal domain of GyrB. Overexpression of YacG results in growth inhibition and alteration in DNA topology due to uncontrolled inhibition of gyrase.
Sengupta
Sugopa
S
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Nagaraja
Valakunja
V
D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D027081:DNA Gyrase / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D029968:Escherichia coli Proteins / Q000378:metabolism*; D059005:Topoisomerase II Inhibitors
D029968:Escherichia coli Proteins; D059005:Topoisomerase II Inhibitors; C465916:YacG protein, E coli; D004247:DNA; D027081:DNA Gyrase