- Craig Kaplan
- Assistant Professor
- BioBio / Room 322A
- BS in Biology, Latin Language and Literature, University of Michigan, 1995.
Ph.D. Harvard University, 2003
- Postdoc: University of Utah, (2003-2004)
- Postdoc:Stanford University (2004-2009)
- Joined Texas A&M in 2009
Mechanism and regulation of transcription by RNA Polymerase II
Control of gene expression in eukaryotes relies on complex regulatory machinery dedicated to proper transcription by RNA Polymerase II (Pol II). My lab focuses on the mechanism and regulation of Pol II enzymatic activity and how it can impact all three phases of transcription: initiation, elongation, and termination. Appropriate regulation of transcription is critical for cellular and organismal development, and is also essential for the prevention of disease states such as cancer. We study Pol II regulation using the model organism, Saccharomyces cerevisiae (Baker’s yeast). This single-celled organism is amenable to genetic, biochemical, genomic and high-throughput approaches, thus we are able to approach mechanism in vivo and in vitro.
One goal of my lab is determining the roles and mechanisms of transcription elongation factors that directly impact Pol II activity, as well as those that coordinate Pol II activity with other co-transcriptional processes, such as RNA processing or epigenetic marking of the chromatin template in vivo. We have taken a genome-scale high-throughput genetic approach for the identification of such factors. Additionally, we are interested in the basic mechanism of Pol II substrate selection and how it may be compromised by natural products such as the mushroom toxin alpha-amanitin. Substrate selection is a key determinant for proper elongation rate and faithful transcription, while molecules that alter or inhibit substrate selection could represent novel classes of anti-fungal or therapeutic drugs.
- Schweikhard, V, Meng, C, Murakami, K, Kaplan, CD, Kornberg, RD, Block, SM (2014) Transcription factors TFIIF and TFIIS promote transcript elongation by RNA polymerase II by synergistic and independent mechanisms. Proc. Natl. Acad. Sci. U.S.A. :
- Pai, DA, Kaplan, CD, Kweon, HK, Murakami, K, Andrews, PC, Engelke, DR (2014) RNAs nonspecifically inhibit RNA polymerase II by preventing binding to the DNA template. RNA 20: 644-55
- Viktorovskaya, OV, Engel, KL, French, SL, Cui, P, Vandeventer, PJ, Pavlovic, EM, Beyer, AL, Kaplan, CD, Schneider, DA (2013) Divergent contributions of conserved active site residues to transcription by eukaryotic RNA polymerases I and II. Cell Rep 4: 974-84
- Braberg, H, Jin, H, Moehle, EA, Chan, YA, Wang, S, Shales, M, Benschop, JJ, Morris, JH, Qiu, C, Hu, F, Tang, LK, Fraser, JS, Holstege, FC, Hieter, P, Guthrie, C, Kaplan, CD, Krogan, NJ (2013) From structure to systems: high-resolution, quantitative genetic analysis of RNA polymerase II. Cell 154: 775-88
- Kaplan, CD (2013) Basic mechanisms of RNA polymerase II activity and alteration of gene expression in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1829: 39-54
- Kaplan, CD, Jin, H, Zhang, IL, Belyanin, A (2012) Dissection of Pol II trigger loop function and Pol II activity-dependent control of start site selection in vivo. PLoS Genet. 8: e1002627
- Larson, MH, Zhou, J, Kaplan, CD, Palangat, M, Kornberg, RD, Landick, R, Block, SM (2012) Trigger loop dynamics mediate the balance between the transcriptional fidelity and speed of RNA polymerase II. Proc. Natl. Acad. Sci. U.S.A. 109: 6555-60
- Murakami, K, Gibbons, BJ, Davis, RE, Nagai, S, Liu, X, Robinson, PJ, Wu, T, Kaplan, CD, Kornberg, RD (2012) Tfb6, a previously unidentified subunit of the general transcription factor TFIIH, facilitates dissociation of Ssl2 helicase after transcription initiation. Proc. Natl. Acad. Sci. U.S.A. 109: 4816-21
- Hartzog, GA, Kaplan, CD (2011) Competing for the clamp: promoting RNA polymerase processivity and managing the transition from initiation to elongation. Mol. Cell 43: 161-3
- Suh, MH, Meyer, PA, Gu, M, Ye, P, Zhang, M, Kaplan, CD, Lima, CD, Fu, J (2010) A dual interface determines the recognition of RNA polymerase II by RNA capping enzyme. J. Biol. Chem. 285: 34027-38