When I first learned about DNA, I was fascinated with the question of how a compound with such simplicity could give us all the diversity we see in the world. It was with that question in mind that I chose to venture into biochemistry. After completing my undergraduate degree in Biochemistry here at Trinity, I went on to obtain a doctoral degree in Molecular Biophysics at the Johns Hopkins University with David E. Draper. I then crossed the country to San Francisco for a postdoctoral fellowship at University of California, San Francisco with Christine Guthrie. Each experience brought me a new set of tools to approach my questions, which had only grown in complexity with the more I learned. All along the way, I was also continually reminded how much I loved the interplay between teaching and research. Therefore, I sought out positions where teaching and research were partnered. This brought me back to Texas, and ultimately to Trinity.
Ph.D. in Molecular Biophysics, John Hopkins University
B.S. in Biochemistry, Trinity University
C.C. Schreib, E.K. Bowman, C.A. Hernandez, A.L. Lucas, C.H.S. Potts, and C. Maeder. (2018) Functional and Biochemical Characterization of Dib1’s Role in Splicing, Journal of Molecular Biology, 430(11): 1640-1651.
A. Gujjari, B.V. Rodriguez, J. Pescador, C. Maeder, G.W. Beall and L.K. Lewis (2018)Factors affecting the association of single- and double-stranded RNAs with montmorillonite nanoclays, International Journal of Biological Macromolecules, 109:551-559.
B.V. Rodriguez, E.T. Malczewskyj, J.M. Cabiya, L.K. Lewis and C. Maeder (2016) Identification of RNase-resistant RNAs in Saccharomyces cerevisiae extracts: separation from chromosomal DNA by selective precipitation. Anal. Biochem. 492, 69-75.
B.V. Rodriguez, J. Pescador, N.Pollok, G.W. Beall, C. Maeder and L. K. Lewis (2015). Impact of size, secondary structure and counterions on the binding of small RNAs to layered double hydroxide nanoparticles. Biointerphases. 10(4): 041007.
J. Abelson, M. Blanco, M.A. Ditzler, F. Fuller, P. Aravamudhan, M. Wood, T. Villa, D.E. Ryan, J.A. Pleiss, C. Maeder, C. Guthrie, N.G. Walter (2010). Conformational Dynamics of single pre-mRNA molecules during in vitro splicing. Nat. Struct. Mol. Biol. 17(4): 504-512.
L. Zhang, T. Xu, C. Maeder, L. Bud, J. Shanks, J. Nix, C. Guthrie, J.A. Pleiss, and R. Zhao (2009) Structural Evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2. Nat. Struct. Mol. Biol. 16(7): 731-739.
C. Maeder*, A.K. Kutach*, and C. Guthrie (2009). ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 Helicase requires the C-terminus of Prp8. Nat. Struct. Mol. Biol. 16(1): 42-8. *equal contributions.
C. Maeder, G.L. Conn, and D.E. Draper (2006). Optimization of a Ribosomal Structural Domain by Natural Selection. Biochemistry, 45(21): 6635-43.
C. Maeder and D.E. Draper (2005). A small protein unique to bacteria organizes rRNA tertiary structure over an extensive region of the 50S ribosomal subunit. J. Mol. Biol., 354 (2): 436-46.
Research in the Maeder Lab centers on characterizing a key mechanism in gene expression, pre-messenger RNA splicing. Splicing precisely removes non-protein coding sequences from RNA prior to translation into proteins. The mechanism involves large-scale rearrangements of protein-RNA complexes, which must be regulated to ensure both splicing timing and accuracy. Our current work focuses on identifying the mechanisms by which several essential splicing proteins regulate spliceosome assembly and activation. We use a variety of biochemical, molecular biological, and genetics techniques to dissect the importance of protein-nucleic acid and protein-protein interactions in the spliceosome.