Office: R424 Research Building
Telephone: (314) 516-7013
B. S. Biology, B. S. Chemistry, 1997, Truman State University, Kirksville, MO.
Ph.D., Biochemistry, 2002, University of Wisconsin, Madison, WI
Postdoctoral fellow, 2002-2005, University of Wisconsin, Madison, WI
Postdoctoral fellow, 2006-2010, University of North Carolina, Chapel Hill, NC
Proper control of gene expression is critical for the development and survival of all organisms as misregulation can lead to disease, including cancer. In my lab we study regulation of gene expression at the post-transcriptional level. Specifically, we investigate 3 end processing of canonical polyadenylated (poly(A)) and histone pre-mRNAs. To study these phenomena, we employ a broad range of cell biological, molecular biological, biochemical, genetic and structural biological techniques. After most protein-coding pre-mRNAs are transcribed by RNA polymerase II (polII), their 3 ends are cleaved and polyadenylated. Interestingly, the replication-dependant histone pre-mRNAs are not polyadenylated following cleavage at the 3end. We have recently determined that a core cleavage complex containing the proteins CPSF73, CPSF100 and Symplekin is responsible for 3 end processing of both poly(A) and histone pre-mRNAs. We also learned that this complex interacts with different accessory proteins when processing poly(A) and histone pre-mRNAs. Work in my lab will continue to focus on this cleavage complex with an ultimate goal of understanding how these proteins function together to process pre-mRNAs.
Kennedy, S. A., Frazier, M. L., Steiniger, M., Mast, A. M., Marzluff, W. F. and Redinbo, M. R., (2009) Crystal Structure of the HEAT Domain from the Pre-mRNA Processing Factor Symplekin. J. Mol. Biol., 392, 115-28.
Sullivan, K. D.*, Steiniger, M.* and Marzluff, W. F., (2009) A core complex of CPSF73, CPSF100, and Symplekin may form two different cleavage factors for processing of poly(A) and histone mRNAs. Molecular Cell, 34, 322-332. (*co-first authors)
Steiniger, M., Metzler, J. D., Reznikoff, W. S., (2006) Mutation of Tn5 Transposase beta-loop residues affects all steps of Tn5 transposition: the role of conformational changes in Tn5 transposition. Biochemisty. 45, 15552-62.
Steiniger, M., Adams, C. D., Marko, J., Reznikoff, W. S., (2006) Defining characteristics of Tn5 Transposase non-specific DNA binding. Nuc. Acids Res. 34, 2820-32.