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Nucleic Acids Research Advance Access originally published online on June 27, 2008
Nucleic Acids Research 2008 36(13):4310-4316; doi:10.1093/nar/gkn355
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Nucleic Acids Research, 2008, Vol. 36, No. 13 4310-4316
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

YacG from Escherichia coli is a specific endogenous inhibitor of DNA gyrase

Sugopa Sengupta1 and Valakunja Nagaraja1,2,*

1Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012 and 2Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore-560064, India

*To whom correspondence should be addressed. Tel: +91 80 2360 0668; Fax: +91 80 2360 2697; Email: vraj{at}mcbl.iisc.ernet.in

Received March 27, 2008. Revised May 17, 2008. Accepted May 19, 2008.

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.


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