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A Region of Bacillus subtilis CodY Protein Required for Interaction with DNA

Pascale Joseph, Manoja Ratnayake-Lecamwasam, and Abraham L. Sonenshein^*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 13 October 2004/ Accepted 10 March 2005

Bacillus subtilis CodY protein is the best-studied member of a novel family of global transcriptional regulators found ubiquitously in low-G+C gram-positive bacteria. As for many DNA-binding proteins, CodY appears to have a helix-turn-helix (HTH) motif thought to be critical for interaction with DNA. This putative HTH motif was found to be highly conserved in the CodY homologs. Site-directed mutagenesis was used to identify amino acids within this motif that are important for DNA recognition and binding. The effects of each mutation on DNA binding in vitro and on the regulation of transcription in vivo from two target promoters were tested. Each of the mutations had similar effects on binding to the two promoters in vitro, but some mutations had differential effects in vivo.

Present address: Corporate-Sponsored Research and Licensing, Massachusetts General Hospital, Charlestown, MA 02129.

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