Professor of Biochemistry and Molecular Biology, University of Massachusetts
Ph.D.: University of Chicago
Vierling Lab 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.
Kim, M., U. Lee, I. Small, C. des Francs-Small, E. Vierling. Mutations in a mitochondrial transcription termination factor (mTERF)-related protein enhance thermotolerance in the absence of the major molecular chaperone HSP101. Plant Cell, in press. (2012).
Stengel,F., A. J. Baldwin, M. F. Bush, G. R. Hilton, H. Lioe, E. Basha, N. Jaya, E. Vierling, J. L.P. Benesch. Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach. Chem. Biol. 19: 599-607 (2012).
Basha, E., H. O’Neill, E. Vierling. Small Heat Shock Proteins/α-crystallins:Dynamic proteins with flexible functions. Trends Biochem. Sci. 37:106-117 (2012).
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]