Office: BMSB 824
Phone: (405) 271-2227 ext. 61248
Fax: (405) 271-3092
940 S. L. Young Blvd., BMSB 824
Oklahoma City, OK 73104
PhD, University of Illinois Urbana-Champaign, 1991
Structural and functional studies of proteins that catalyze V(D)J recombination: Mechanisms of regulation and maintenance of genomic stability.
Recognition of foreign antigens in the human immune system is primarily performed by the B and T cell receptors. The genes encoding the antigen-binding receptors are produced in a functional form during specific stages of lymphocyte development through a specific DNA rearrangement process referred to as V(D)J recombination. The initial step in V(D)J recombination is site-specific DNA cleavage that is catalyzed by the RAG1 and RAG2 proteins. Mutations in either RAG protein that disrupt catalytic activity results in fatal immunodeficiency diseases. On the other hand, aberrant activity leading to DNA cleavage at incorrect genomic sites can result in chromosomal translocations leading to the development of certain lymphomas and leukemias. In this laboratory, we are characterizing the factors that catalyze V(D)J recombination at the molecular level using biochemical and structural biology methods, as well as using a variety of methods to elucidate RAG protein function and interactions at the cellular level.
- Rodgers, K.K. (2017) Riches in RAGS: Revealing the V(D)J recombinase through high resolution structures. Trends Biochem. Sci., 42, 72-84.
- Rodgers, W., Byrum, J.N., Sapkota, H., Rahman, N.S., Cail, R.C., Zhao, S., Schatz, D.G., and Rodgers, K.K. (2015) Spatio-temporal regulation of RAG2 following genotoxic stress. DNA Repair, 27, 19-27.
- Byrum, J.N., Zhao, S., Rahman, N.S., Gwyn, L.M., Rodgers, W., and Rodgers, K.K. (2015) An interdomain boundary in RAG1 facilitates cooperative binding to RAG2 in formation of the V(D)J recombinase complex. Protein Science, 24, 861-873.
- Arbuckle, J.L., Rahman, N.S., Zhao, S., Rodgers, W., and Rodgers, K.K. (2011) Elucidating the domain architecture and functions of non-core RAG1: The capacity of a non-core zinc-binding domain to function in nuclear import and nucleic acid binding. BMC Biochem., 12, 23.
- Gwyn, L.M., Peak, M.M., De, P., Rahman, N.S., and Rodgers, K.K. (2009) A zinc site in the C-terminal domain of RAG1 is essential for DNA cleavage activity. J. Mol. Biol., 390, 863-878.
- Zhao, S., Gwyn, L.M., De, P., and Rodgers, K.K. (2009) The non-sequence specific DNA binding mode of RAG1 is inhibited by RAG2. J. Mol. Biol., 387, 744-758.
- Rahman, N.S., Godderz, L.J., Stray, S., Capra, J.D., and Rodgers, K.K. (2006) DNA cleavage of a cryptic recombination signal sequence by RAG1 and RAG2: Implications for partial VH gene replacement. J. Biol. Chem., 281, 12370-12380.
- De, P., and Rodgers, K.K. (2004) DNA cleavage activity of the V(D)J recombination protein RAG1 is autoregulated. Mol. Cell. Biol., 24, 6850-6860
- De, P., and Rodgers, K.K. (2004) Putting the pieces together: Identification and characterization of structural domain in the V(D)J recombination protein RAG1. Immunol. Rev., 200, 70-82.
- Peak, M.M., Arbuckle, J.L., Rodgers, K.K., (2003) The central domain of core RAG1 preferentially recognizes single-stranded RSS heptamer. J. Biol. Chem., 278, 18235-18240.
- Godderz, L.J., Rahman, N.S., Risinger, G.M., Arbuckle, J.L., Rodgers, K.K., (2003) Self-association and conformational properties of RAG1: Implications for formation of the V(D)J recombinase. Nucl. Acids Res., 31, 2014-2023.
- Arbuckle, J.L., Fauss, L.J., Simpson, R., Ptaszek, L.M., Rodgers, K.K., (2001) Identification of two topologically independent domains in RAG1 and their role in macromolecular interactions relevant to V(D)J recombination. J. Biol. Chem., 276, 37093-37101.
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