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.
Basha, E., H. O’Neill, E. Vierling. Small Heat Shock Proteins/α-crystallins:Dynamic proteins with flexible functions. Trends Biochem. Sci. (2011) Dec 14. [Epub ahead of print]. [PubMed]
Benesch, J.L.P., J A. Aquilina, A. J. Baldwin, A. Rekas, F. Stengel, R. A Lindner, E. Basha, G. L. Devlin, J. Horwitz, E. Vierling, J. A. Carver, & C. V. Robinson. The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chem. Biol. 17:1008-1017 (2010). [Link]
Basha, E., C. Jones, V. Wysocki, E. Vierling. Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol. J. Biol. Chem. 285:11489-11497 (2010). [Link]
Stengel, F., A. J. Baldwin, A. J. Painter, N. Jaya, E. Basha, L. E. Kay, E. Vierling, C. V. Robinson, J. L.P. Benesch. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc. Natl. Acad. Sci. 107:2007-2012 (2010). Featured in PNAS commentary: 107:2727-2728. [Link]
Jaya, N., V. Garcia*, E. Vierling. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc. Natl. Acad. Sci. 106:15604-15609 (2009). [Link]
Cheng, G., E. Basha, V.H. Wysocki, E. Vierling. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem., 283:26634-42 (2008) Featured as "Paper of the Week". [PubMed]
Lee, U., C.Wie*, B. O. Fernandez, M. Feelisch, E. Vierling. Modulation of nitrosative stress by S-nitrosoglutathione reductase is critical for thermotolerance and plant growth. Plant Cell 20: 786-802, (2008).[PubMed]
Tonsor, S.J., C. Scott, I. Boumanza*, T.R. Liss, J.L. Brodsky, E. Vierling. Heat shock protein 101 effects in Arabidopsis thaliana: Genetic variation, fitness and pleiotropy in controlled environments. Mol. Ecol., 17: 1614-1626 (2008). [PubMed]
Larkindale, J., E. Vierling. Core genome responses involved in acclimation to high temperature. Plant Physiol. 146: 748-761 (2008). [PubMed]
Siddique, M., S. Gernhard, P. von Koskull-Döring, E. Vierling, K-D. Scharf. The plant sHSP superfamily: Five new members in Arabidopsis thaliana with unexpected properties. Cell Stress & Chaperones 13:183-197 (2008).[PubMed]
McClellan, C.A., T.J. Turbeyville, E.M. K. Wijeratne, A. Kerschen, E. Vierling, C. Queitsch, L. Whitesell, A.A. Gunatilaka. A rhizosphere fungus enhances Arabidopsis thermotolerance through production of an Hsp90 inhibitor. Plant Physiol 145: 174-182 (2007). Highlighted in Science Stke. [Link]
Lee, U., I. Rioflorido, S-W. Hong, J. Larkindale, E. R.Waters, E.Vierling. The Arabidopsis ClpB/Hsp100 family of proteins: Chaperones for stress and chloroplast development. Plant Journal 49:115-127 (2007). [Link]