Laura Romberg

  • Associate Professor of Biology

Areas of Study


  • BA, Princeton University, 1989
  • PhD, Univ California San Francisco, 1997


Professor Romberg is a member of the Department of Biology and an affiliate of the Department of Chemistry and Biochemistry.

Specialties: bacterial cell division, the biochemistry of the cytoskeleton

Teaching:  I teach an upper level courses in Microbiology (Biol 306/307) and an advanced seminar in Prokaryotic Cell Biology (Biol 403). I also teach Cell and Molecular Biology (Biol 213/214) and will probably teach a first year seminar on the science of food and cooking.

Outside of my teaching and research, I enjoy swimming, biking, going to art exhibits and art movies, and eating ethnic foods.

The increasing prevalence of drug-resistant bacteria has resulted in searches for new antibiotics. Penicillin inhibits bacterial elongation, but cell division is another potential target that is now being explored. A protein called FtsZ is essential for bacterial cell division and may make a good antibiotic target; it is present in nearly all bacterial species but is absent in humans. As a result, inhibiting FtsZ function could prevent bacteria from dividing without causing side effects due to interactions with human proteins.

FtsZ is a distant homolog of eukaryotic tubulin and polymerizes to form part of the bacterial cytoskeleton. Like the musculoskeletal system of our own bodies, a cell's cytoskeleton determines its shape and can produce force. However, unlike the bones in a skeleton, the structures in the cytoskeleton are transient. The cytoskeleton as a whole is maintained through continual, carefully balanced polymer assembly and disassembly. Understanding FtsZ's polymer dynamics will aid the development of drugs that can disrupt FtsZ structures and thereby prevent cell division.

In cells, FtsZ assembles into a ring at the future site of cell division. This ring is highly dynamic and can rapidly assemble, relocalize, constrict, and disassemble. Ring dynamics are due to the reversibility of FtsZ polymerization; like microtubules, FtsZ polymers assemble in the presence of GTP but tend to curve and disassemble after the GTP has been hydrolyzed.

It is unknown whether FtsZ exhibits the complex, cooperative behaviors of tubulin, including 1) nucleated assembly: the establishment of new polymers is less favorable than growth from pre-established polymers, and 2) dynamic instability: at steady state, individual polymers undergo abrupt transitions between steady growth and rapid shrinkage. My lab is addressing two major questions:1) At what level of assembly does cooperative polymerization emerge? 2) How is FtsZ polymerization promoted or inhibited by its interactions with other proteins?

1. *Miraldi, E., Thomas, P., and Romberg, L. 2008. Allosteric Models for Cooperative Polymerization of Linear Polymers. Biophysical Journal 95: 2470-2486. *undergraduate co-author

2. Margalit D.N., Romberg L., Mets R.B., Hebert A.M., Mitchison T.J., Kirschner M.W., and D. RayChaudhuri. 2004. Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality. Proceedings of the National Academy of Sciences USA. 101(32):11821-6.

3. Romberg, L. and T.J. Mitchison. 2004. Rate-Limiting Guanosine 5'-Triphosphate Hydrolysis during Nucleotide Turnover by FtsZ, a Prokaryotic Tubulin Homologue Involved in Bacterial Cell Division. Biochemistry 43: 282-8.

4. Romberg, L., and P.A. Levin. 2003. Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability. Annual Review of Microbiology 57: 125-54.

5. Romberg, L., M. Simon, and H.P. Erickson. 2001. Polymerization of FtsZ, a bacterial homolog of tubulin - Is assembly cooperative? Journal of Biological Chemistry 276: 11743-11753.

6. Romberg, L., D.W. Pierce, and R.D. Vale. 1998. Role of the kinesin neck region in processive microtubule-based motility. Journal of Cell Biology 140: 1407-16.

7. Vale, R.D., T. Funatsu, D.W. Pierce, L. Romberg, Y. Harada, and T. Yanagida. 1996. Direct observation of single kinesins molecules moving along microtubules. Nature 380: 451-453.

8. Romberg, L., and R.D. Vale. 1993. Chemomechanical cycle of kinesin differs from that of myosin. Nature 361: 168-170.

9. Suter, B., Romberg, L.M., and R. Steward. 1989. Bicaudal-D, a Drosophila gene involved in developmental asymmetry: localized transcript accumulation in ovaries and sequence similarity to myosin heavy chain tail domains. Genes and Development 12A: 1957-68.

Spring 2024

Molecular Biology, Cell Biology, and Biochemistry — BIOL 213
The Cell and Molecular Biology of Pathogen-Host Interactions — BIOL 403

Fall 2024

What's For Dinner? The Science of Healthy Eating — FYSP 022
Microbiology — BIOL 307


Haoyuan Gao Wins Oberlin's 2024 Nexial Prize

June 11, 2024

Haoyuan Gao ’24, a biology and neuroscience double major with minors in book studies, chemistry, and East Asian studies, has been named the winner of Oberlin’s 2024 Nexial Prize. The award is presented to an outstanding science student with aspirations for interdisciplinary research.