Danielle Tullman-Ercek

Ph.D., University of Texas at Austin

Chemical and Biological Engineering
Interdisciplinary Biological Sciences Program

Office Phone: 847.491.7043
Tullman-Ercek Lab


Our focus is to control the transport of all types of materials, from electrons to macromolecules, across cellular membranes. Proteins are the principal "gatekeepers" of the cell but are in relatively complex formations, and therefore we rely heavily on a combination of protein engineering, synthetic biology, and biophysics strategies to achieve our goals. Notably, this permits us to engineer not only lipid-based membrane systems but also those membranes that are composed entirely of proteins. Our model systems include protein compartments such as the MS2 viral capsid and enteric bacterial microcompartments, and traditional membrane protein complexes such as the type III secretion system and multidrug efflux pumps. In the process of trying to engineer these systems to gain or improve function, we often make surprising observations that lead to new, hypothesis-driven basic science projects. Moreover, the changes we introduce in order to achieve altered function often also change the structure of these protein complexes in unpredictable ways, allowing us to develop new design rules for multi-protein assemblies. This work has broad application, from the production of biochemicals to the development of living batteries.

Selected Publications

  1. Evidence for Improved Encapsulated Pathway Behavior in a Bacterial Microcompartment through Shell Protein Engineering. Slininger Lee MF, Jakobson CM, Tullman-Ercek D. ACS Synthetic Biology. 2017 Jun 21.
  2. A Secretion-Amplification Role for Salmonella enterica Translocon Protein SipD. Glasgow AA, Wong HT, Tullman-Ercek D. ACS Synthetic Biology. 2017 Jun 16;6(6):1006-1015.
  3. De novo design of signal sequences to localize cargo to the 1,2-propanediol utilization microcompartment. Jakobson CM, Slininger Lee MF, Tullman-Ercek D. Protein Science. 2017 May;26(5):1086-1092.
  4. Proteins adopt functionally active conformations after type III secretion. Metcalf KJ, Bevington JL, Rosales SL, Burdette LA, Valdivia E, Tullman-Ercek D. Microbial Cell Factories. 2016 Dec 23;15(1):213.
  5. A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle. Asensio MA, Morella NM, Jakobson CM, Hartman EC, Glasgow JE, Sankaran B, Zwart PH, Tullman-Ercek D. Nano Letters. 2016 Sep 14;16(9):5944-50.
  6. Dumpster Diving in the Gut: Bacterial Microcompartments as Part of a Host-Associated Lifestyle. Jakobson CM, Tullman-Ercek D. PLoS Pathogens. 2016 May 12;12(5):e1005558.
  7. Type-III secretion filaments as scaffolds for inorganic nanostructures. Azam A, Tullman-Ercek D. Journal of the Royal Society Interface. 2016 Jan;13(114):20150938.
  8. Localization of Proteins to the 1,2-Propanediol Utilization Microcompartment by Non-native Signal Sequences Is Mediated by a Common Hydrophobic Motif. Jakobson CM, Kim EY, Slininger MF, Chien A, and Tullman-Ercek D. Journal of Biological Chemistry. 2015 October 2;290(40):24519-24533.
  9. Influence of Electrostatics on Small Molecule Flux through a Protein Nanoreactor. Glasgow JE, Asensio MA, Jakobson CM, Francis MB, Tullman-Ercek D. ACS Synthetic Biology. 2015 Sep 18;4(9):1011-9.
  10. The effects of time, temperature, and pH on the stability of PDU bacterial microcompartments. Kim EY, Slininger MF, Tullman-Ercek D. Protein Science. 2014 Oct;23(10):1434-41.


Recent Photos

July 26, 2017