PhD: University of Chicago
Postdoctoral training: University of Georgia, Athens
My research interests are primarily in processes that occur post-transcriptionally and post-translationally to regulate cell function.
A major component of our research program is aimed at understanding the mechanism of action and biological roles of molecular chaperones. Molecular chaperones are a structurally diverse group of highly conserved proteins that share the capacity to bind substrate proteins that are in non-native states. This interaction can facilitate proper protein folding and maturation, protein targeting and dissolution of protein aggregates formed due to stress or disease, giving chaperones a broad impact on normal cell function and stress responses. We have focused on the structure and function of the small heat shock proteins and the HSP100 class of chaperones. In addition, we have an expanding program investigating factors other than chaperones that are essential for organismal stress tolerance, including new work on an enzyme involved in nitric oxide (NO) metabolism, and efforts to understand translational regulation during stress. In striving to address basic biological questions, our research extends from biochemical and protein structural studies to molecular and classical genetic analysis. Our current studies utilize Arabidopsis thaliana and the cyanobacterium Synechocystis sp. PCC6803 as model organisms.
Fionn McLoughlin, Minsoo Kim, Richard S Marshall, Richard D. Vierstra, Elizabeth VierlingProtein disaggregation after heat stress. Plant Physiology May 2019, pp.00263.2019; DOI: 10.1104/pp.19.00263
Santhanagopalan, I., M.T. Degiacomi, D.A. Shepard, G.K.A. Hochberg, J.L.P. Benesch, E. Vierling. It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate. J. Biol. Chem. 293: 19511–19521 (2018). Cover article.
Wang, X., L. Hou, Y. Lu, B. Wu, X. Gong, M. Liu, J. Wang, Q. Sun, E. Vierling, S. Xu. Metabolic adaptation of wheat grain contributes to stable filling rate under heat stress. J. Exp. Bot. 69: 5531-5545 (2018). https://doi.org/10.1093/jxb/ery303
Marklund, E. G., Y. Zhang, E. Basha, J. L.P. Benesch, E. Vierling. Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis. Cell Stress & Chaperones https://doi.org/10.1007/s12192-018-0884-3 (2018). PMCID: PMC6045555
Hochberg, G. K.A., D. A. Shepherd, E.G. Marklund, I. Santhanagoplan, M. Degiacomi, A. Laganowksy, T. M. Allison, E. Basha, M. T. Marty, M. R. Galpin, W. B. Struwe, A. J. Baldwin, E. Vierling, J. L.P. Benesch.. Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science 359: 930-935 (2018). PMID:29472485
Guerra, D., S. Eyles, I. Truebridge, P. Treffon, E. Vierling. Direct detection of in vitro protein nitrosation by mass spectrometry: S-Nitrosoglutathione Reductase as a Model Protein. In: Mengel A., Lindermayr C. (eds) Nitric Oxide. Methods in Molecular Biology, vol 1747, pp 143-160. Humana Press, New York, NY (2018). PMID:29600457