Jennifer Ottesen

Jennifer Ottesen
Jennifer Ottesen
Associate Professor
Divisional Affiliation: Biochemistry
Office: 780 Biosciences Building
Phone: 614-292-4525


Research Overview

Research in the Ottesen laboratory utilizes peptide and protein chemistry to address biological problems. The Ottesen group is developing improved techniques for solid phase chemical ligation, which allows the rapid recombination of peptide elements into larger macromolecules. They also employ expressed protein ligation, in which synthetic polypeptides and recombinant protein elements can be chemoselectively linked together. This allows the power of synthetic techniques to be applied to large proteins. 


Howard, C.J., Yu, R.R., Gardner, M.L., Shimko, J.C., *Ottesen, J.J. “Chemical and Biological Tools for the Preparation of Modified Histone Proteins” (2015). Top. Curr. Chem. 363, 193-226.

Brehove, M., Wang, T., North, J., Luo, Y., Dreher, S.J., Shimko, J.C., Ottesen, J.J., Luger, K., Poirier, M.G., “Histone Core Phosphorylation Regulates DNA Accessibility”, (2015). J. Biol. Chem. 290(37), 22612-22621.

Bernier, M. ,Luo, Y., Nwokelo, K.C., Goodwin, M., Dreher, S.J., Zhang, P., Parthun, M.R., Fondufe-Mittendorf, Y.N., Ottesen, J.J., Poirier, M.G., “Linker histone H1 and H3K56 Acetylation Are Antagonistic Regulators of Nucleosome Dynamics”, (Nat. Commun., accepted with minor revisions)

Chatterjee, N., North, J.A., Dechassa, M.L., Manohar, M., Prasad, R., Luger, K., Ottesen, J.J., Poirier, M.G., Bartholomew, B.B. “Histone acetylation near the nucleosome dyad axis enhances nucleosome disassembly by RSC and SWI/SNF (2015). Mol. Cell. Biol., ePub Sep 28, MCB.00441-15.

North, J.A., Simon, M., Ferdinand, M.B., Shoffner, M.A., Picking, J.W., Howard, C.J., Mooney, A.M., van Noort, J., *Poirier, M.G., and *Ottesen, J.J. “Histone H3 Phosphorylation Near the Nucleosome Dyad Alters Chromatin Structure” (2014). Nucleic Acids Research, 42(8), 4922-4933.

Shimko, J.C., Howard, C.J., Poirier, M.G., and *Ottesen, J.J. “Preparing Semisynthetic and Fully Synthetic Histones H3 and H4 to Modify the Nucleosome Core” in volume “Protein Acetylation: Methods and Protocols” (2013) of Methods in Molecular Biology, 981, 177-192. DOI: 10.1007/978-1-62703-305-3_14.

North, J.A., Shimko, J.C., Javaid, S., Mooney, A.M., Shoffner, M.A., Rose, S.D., Bundschuh, R., Fishel, R., Ottesen, JJ. and *Poirier, J.G.; “Regulation of the Nucleosome Unwrapping Rate Controls DNA Accessibility”, (2012). Nucleic Acids Research, 40(20), 10215-10227. DOI:10.1093/nar/gks747

Mahto, S.K., Howard, C.J., Shimko, J.C., and *Ottesen, J.J.; “A Reversible Protection Strategy to Improve Fmoc-SPPS of Peptide Thioesters by the N-Acylurea Approach”, (2011). ChemBioChem, 12. 2488-2494. DOI: 10.1002/cbic.201100472.

Simon, M., North, J.A., Shimko, J.C., Forties, R.A., Ferdinand, M.B., Manohar, M., Zheng, M., Fishel, R., *Ottesen, J.J., *Poirier, M.G., (2011). “Histone Fold Modifications Control Nucleosome Unwrapping and Disassembly”, Proc. Nat. Acad. Sci. USA, 108(31), 12711-12716. DOI: 10.1073/pnas.1106264108.

Shimko, J.C., North, J., *Poirier, M.G., *Ottesen, J.J., “Preparation of Fully Synthetic Histone H3 Reveals that Acetyl-Lysine 56 Facilitates Protein Binding Within Nucleosomes”, (2011). J. Mol. Biol., 408(2), 187-204. DOI: 10.1016/j.jmb.2011.01.003

North, J.A., Javaid, S., Ferdinand, M.B., Chatterjee, N., Picking, J.W., Shoffner, M., Nakkula, R.J, Bartholomew, B., *Ottesen, J.J., *Fishel, R., and *Poirier, M.G., “Phosphorylation of Histone H3(T118) Alters Nucleosome Dynamics and Remodeling”, (2011) Nucleic Acids Research, 39(15), 6465-6474. DOI: 10.1093/nar/gkr304

Javaid, S., Manohar, M., Punja, H., Mooney, A., *Ottesen, J.J., *Poirier, M.G., *Fishel, R.A. “Nucleosome remodeling catalyzed by the human hMSH2-hMSH6 Mismatch Recognition Complex”, (2009). Mol. Cell., 36, 1086-1094. DOI: 10.1016/j.molcel.2009.12.010

Li, X., Fekner, T., Ottesen, J.J., Chan, M.K. “A Pyrrolysine Analog for Site-Specific Protein Ubiquitination”, (2009). Angew. Chem., 48(48), 9184-9187. DOI: 10.1002/anie.200904472.

Manohar, M., Mooney, A.M., Picking, J.W., Edon, A. Nakkula, R.J., Fishel, R.A., *Poirier, M.G., and *Ottesen, J.J. (2009). Acetylation of Histone H3 at the Nucleosome Dyad Reduces DNA-Histone Binding, J. Biol. Chem., 284, 23312-23321. DOI: 10.1074/jb.M109.003202

Ottesen, J.J., Bar-Dagan, M., Giovani, B., Muir, T.W.  (2008) "An amalgamation of solid phase peptide synthesis and ribosomal peptide synthesis." Biopolymers 90(3):406-14.

Ottesen, J.J., Huse, M., Sekedat, M.D., Muir, T.W.  (2004) "Semisynthesis of phosphovariants of Smad2 reveals a substrate preference of the activated T beta RI kinase." Biochemistry 43(19), 5698-706.

Cowburn, D., Shekhtman, A., Xu, R., Ottesen, J.J., Muir, T.W.  (2004) "Segmental isotopic labeling for structural biological applications of NMR." Methods Mol Biol. 278, 47-56.

Wilson, K.A., Kalkum, M., Ottesen, J.J., Yuzenkova, J., Chait, B.T., Landick, R., Muir, T., Severinov, K. and Darst, S.A.  (2004) "Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail." J. Am Chem. Soc. 125(41), 12475-83.

Ottesen, J.J., Blaschke, U.K. Cowburn, D. and Muir, T.W. (2003) "Segmental isotopic labeling:  Prospects for a new tool to study the structure-function relationships in multi-domain proteins."  Biol. Mag. Res. 20, 35-51.

Mezo, A.R., Ottesen, J.J., and Imperiali B.  (2001) " Discovery and characterization of a discretely folded homotrimeric betabetaalpha peptide." J. Am. Chem. Soc. 123(5), 1002-3.

Ottesen, J.J. and Imperiali, B.  (2001) " Design of a discretely folded mini-protein motif with predominantly beta-structure." Nat. Struct. Biol.8(6), 535-9.

Imperiali, B. and Ottesen, J.J.  (1999) "Uniquely folded mini-protein motifs." J. Pept. Res. 54(3), 177-84. (Review)

Imperiali, B. and Ottesen, J.J.  (1998) "Design strategies for the construction of independently folded polypeptide motifs." Biopolymers 47(1), 23-9.

Struthers, M., Ottesen, J.J.and Imperiali B.  (1998) "Design and NMR analyses of compact, independently folded BBA motifs." Fold Des. 3(2), 95-103.