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Our group is also studying three proteins that interact with DNA. We are pursuing the structures of the proteins in isolation and also in complexes with DNA. The first protein is the replication terminator protein( RTP) from Bacillus subtilis. RTP recognizes and binds a tandem array of specific sites on the B. subtilis genome, and this arrangement sequesters the termination of DNA replication to a specific locus to prevent the buildup of mutations within the genome. We have solved the crystal structure of RTP in isolation and are currently growing crystals of the RTP-DNA termination complex. The second protein is MotA, a phage T4 transcription factor that controls the expression of T4 middle genes. We have characterized the DNA-binding domain by NMR spectroscopy and are about to start crystallization trials of the domain in complex with DNA. Finally, we have started work on the DNA-binding domain of human CP2, a transcription factor that is involved in the regulation of the globin genes.
Last update: April 2003