• Primary Faculty Profiles
• Bankert, Richard, Ph.D., V.M.D., Professor
• Bianco, Piero, Ph.D., Associate Professor
• Campagnari, Anthony, Ph.D., Professor
• Collins, Arlene, Ph.D., Associate Professor
• Connell, Terry, Ph.D., Professor
• Egilmez, Nejat, Ph.D., Associate Professor
• Hakansson, Anders, Ph.D., Assistant Professor
• Hay, John, Ph.D., Professor
• Jacobs, Amy, Ph.D., Assistant Professor
• Melendy, Thomas, Ph.D., Associate Professor
• Panepinto, John, Ph.D., Assistant Professor
• Read, Laurie, Ph.D., Professor
• Russell, Michael, Ph.D., Professor
• Ruyechan, William, Ph.D., Professor and Chairman
• Thacore, Harshad, Ph.D., Associate Professor
• Williams, Noreen, Ph.D., Professor
• Adjunct Faculty Profiles
• Departmental Publications
• Career Opportunities
• The Witebsky Center
• Seminars

Faculty and Research

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Research Interests:

Mechanistic studies of DNA double strand break repair

The work in my group focuses on the biochemical mechanism of DNA double strand break repair.  To understand this complex process, we utilize a combination of physical biochemical and single molecule biophysical techniques.  For single molecule studies, we use a combination of optical tweezers, fluorescence microscopy and laminar flow cells to isolate individual molecules of DNA and observe the action of the repair machinery in real time.  We then make movies of the molecular machinery in action and then conduct detailed analyses to extract information of the mechanism in action.

To understand DNA double strand break repair, the lab is divided into 3 groups, arranged according to organism.

1. Escherichia coli – here we focus on the DNA molecular motors RecG, RuvAB and RecBCD. This group uses these enzymes to understand how DNA helicases interact with and process their DNA substrates to facilitate repair of damaged chromosomes.
2. C. elegans – here we study the interaction between the breast cancer associated gene Brc2 and the DNA strand exchange protein, Rad51. We selected C. elegans as a model system as the Brc2 homologue is manageable and posses all of the components of its significantly larger human counterpart.
3. H. sapiens – this group focus on the role of the dsDNA translocase Rad54 and its interaction with rad51 and their combined actions in DNA strand exchange.
   

Relevant references:

Brewer, L.R., and Bianco, P.R. (2008). Laminar flow cells for single-molecule studies of DNA-protein interactions. Nature Methods 5, 517-525.

Slocum, S.L., Buss, J.A., Kimura, Y., and Bianco, P.R. (2007). Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA. J. Mol. Biol. 367, 647-664.

Bianco, P.R., Bradfield, J.J., Castanza, L.R., and Donnelly, A.N. (2007). Rad54 oligomers translocate and cross-bridge double-stranded DNA to stimulate synapsis. J. Mol. Biol. 374, 618-640.

Kimura, Y., and Bianco, P.R. (2006). Single molecule studies of DNA binding proteins using optical tweezers. The Analyst 131, 868-874.

Handa, N., Bianco, P.R., Baskin, R.J., and Kowalczykowski, S. (2005). Direct Visualization of RecBCD Movement Reveals Cotranslocation of the RecD Motor after χ Recognition. Mol Cell 17, 745-750.

Bianco, P.R. (2004). Hepatitis C NS3 helicase unwinds RNA in leaps and bounds. Lancet 364, 1385-1387.
Spies, M., Bianco, P.R., Dillingham, M.S., Handa, N., Baskin, R.J., and Kowalczykowski, S.C. (2003). A molecular throttle: the recombination hotspot chi controls DNA translocation by the RecBCD helicase. Cell 114, 647-654.

Bianco, P.R., Brewer, L.R., Corzett, M., Balhorn, R., Yeh, Y., Kowalczykowski, S.C., and Baskin, R.J. (2001). Processive translocation and DNA unwinding by individual RecBCD enzyme molecules. Nature 409, 374-378.

Bianco, P.R., and Kowalczykowski, S.C. (2000). Translocation step size and mechanism of the RecBC DNA helicase. Nature 405, 368-372.