Welcome to the Landick Lab

Our research focuses on RNA polymerase, the central enzyme of gene expression in all free-living organisms. Our goal is to understand how RNA polymerase is regulated during the process of transcription (RNA synthesis). In organisms from bacteria to humans, the cell's ability to make long RNA chains, which include most mRNAs and some structural RNAs (e.g., rRNA), requires that extrinsic elongation regulators interact with RNA polymerase to suppress its innate tendency to fall into inactive off-line states that include long pauses, arrest, or termination. We seek to understand the fundamental properties of RNA polymerase that make it susceptible to pausing, arrest, or termination and how elongation regulators alter these properties. We study RNA polymerases from both bacterial and human cells and use a variety of approaches, from genetics to biophysics to structural biology, to study this fundamental paradigm of gene regulation. Lab members are engaged in experiments ranging from detailed biochemical characterization of protein-nucleic acid interactions, to the study of transcription regulators in cells using microarray methods (so-called ChIP chip), to collaborative projects with other labs to study transcription by single molecules of RNA polymerase and to obtain crystallographic sturctures of RNA polymerase and transcription regulators. Our work has practical applications in drug discovery by identification on novel RNA polymerase inhibitors and in controlling transcriptional programs for synthetic microbiology. Follow links here to learn more about our research and our lab.
News
* We've moved to new quarters! In Spring, 2007 we changed academic homes to the Department of Biochemistry at UW-Madison and moved to a new lab in the UW-Madison Microbial Sciences Research Building Oct. 22, 2007. We maintain an affiliation with Bacteriology, which combined with our new affiliation with Biochemistry will strengthen mechanistic aspects of our research especially in single-molecule transcription, while maintaining a strong research focus in Microbiology.
* View our Biochemistry Department Web Page (link)
* Join us. We currently are recruiting new lab members to join ongoing projects. (link)
* Check out our photo page for views of the new lab. (Landick lab photo page)
* Visit our contact page for a map to our new lab. (Contact Us)

Check out our latest publications

Toulokhonov, I., J. Zhang, M. Palangat, and R. Landick. 2007. A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing, Mol. Cell 27, 406-419.    Supplement

Vassylyev, D. G.,, M. N. Vassylyeva, J. Zhang, M. Palangat, I. Artsimovitch, and R. Landick. 2007. Structural basis for substrate loading in bacterial RNA polymerase, Nature 448, 163-168.    Supplement

Kyzer, S. , K. Ha, R. Landick, and M. Palangat. 2007. Direct versus limited-step reconstitution reveals key features of an RNA hairpin-stabilized paused transcription complex, J. Biol. Chem. 282, 19020-19028.

Davis, C. A., C. A. Bingman, R. Landick, M. T. Record, Jr.,and R. M. Saecker 2007. Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymerase, Proc. Natl Acad. Sci. U.S.A. 104, 7833-7388.    Supplement

Landick, R. 2006. A long time in the making - The Nobel Prize for RNA polymerase, Cell 127, 1087-1090.

Toulokhonov, I, and R. Landick. 2006. The role of the lid element in transcription by E. coli RNA polymerase, J. Mol. Biol. 361, 644-658.

Dalal R. V., M. H. Larson, K. C. Neuman, J. Gelles, R. Landick, and S. M. Block. 2006. Pulling on the nascent RNA during transcription does not alter kinetics of elongation or ubiquitous pausing. Mol. Cell . 23, 231-239.

Herbert, K. M. , A. La Porta, B. J. Wong, R. A. Mooney, K. C. Neuman, R. Landick, S. M. Block. 2006. Sequence-resolved detection of pausing by single RNA polymerase molecules. Cell . 125, 1083-1094.

Ederth, J., R. A. Mooney, L. Issakson and R. Landick. 2006. Allosteric interplay between the downstream DNA jaw domain of bacterial RNA polymerase and allele-specific residues in the product RNA-binding pocket, J. Mol. Biol. 365, 1163-1179.

Mooney, R. A., S. A. Darst, and R. Landick. 2005. Sigma and RNA polymerase: an on-again, off-again relationship? Mol. Cell . 20, 335-345.

Abbondanzieri, E. A., W. J. Greenleaf, J. W. Shaevitz, R. Landick, and S. Block. 2005. Direct observation of base-pair stepping by RNA polymerase. Nature . 438, 460-465.    Supplement

Palangat, M. P., D. B. Renner, D. H. Price and R. Landick. 2005. DSIF/NELF, a negative elongation factor for human RNA polymerase II, is a potent inhibitor of the anti-arrest factor TFIIS. Proc. Natl. Acad. Sci. U. S. A. . 102, 315036-15042.

Herring, C. D., M. Raffaelle, T. E. Allen, E. J. Kanin, R. Landick, A. Z. Ansari and B. Ø. Palsson. 2005. Immobilization of Escherichia coli RNA polymerase and location of binding sites by use of chromatin immunoprecipitation and microarrays. .J. Bacteriol. . 187, 6166-6174.

Geszvain, K., and R. Landick. 2005. The structure of bacterial RNA polymerase.
Web Site Edition 12 pp.

Palangat, M., C. T. Hittinger and R. Landick. 2004. Downstream DNA selectively affects a paused conformation of human RNA polymerase II. J. Mol. Biol. 341, 429-441.

R. Landick. 2004. Active-site dynamics in RNA polymerases, Cell . 116, 351-353.

Artsimovitch, I., C. Chu, S. Lynch, and R. Landick. 2003. A new class of bacterial RNA polymerase inhibitor affects nucleotide addition. Science 302,650-654.

Mooney, R. A., and R. Landick. 2003. Tethering sigma70 to RNA polymerase reveals high in vivo activity of sigma factors and sigma70-dependent pausing at promoter-distal location, Genes Dev. 17, 2839-2851.   Supplement

Toulokhonov, I, and R. Landick. 2003. The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination. Mol. Cell 12, 1125-1136.   Supplement