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Elizabeth Vierling

Distinguished Professor

My research interests are in post-transcriptional and post-translational processes that regulate cell function in response to stress, including the action of molecular chaperones in protein homeostasis, nitric oxide homeostasis, and control of reactive oxygen species. I am also involved in a new project aimed at mining the diversity of plant specialized metabolism for molecules that could be used as antimicrobials or other therapeutics.

Current Research
A major goal of our work is to understand the mechanism of action and biological roles of molecular chaperones, in particular the alpha-crystallin related small heat shock proteins and the protein disaggregase Hsp101. Molecular chaperones are structurally diverse, highly conserved proteins that 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 cell function and stress responses. In addition, we have expanding investigations of other factors essential for organismal stress tolerance, including an enzyme of nitric oxide metabolism enzyme [S-nitrosoglutathione reductase (GSNOR)], regulation of mitochondrial metabolism, and translational control during stress. In striving to address basic biological questions, our research extends from biochemical and protein structural studies to molecular and classical genetic analysis using Arabidopsis thaliana and the cyanobacterium Synechocystis sp. PCC6803 as model organisms.

I am also involved in a new, collaborative project to mine diverse plant species for natural products. This research draws on a collection of plant tissue culture samples from close to 3000 different species that was recently donated to UMass from industry. We intend to use the collection for compound extraction and RNA-seq to uncover new molecules of medicinal and industrial value.

Learn more at

Academic Background:

  • BS University of Michigan, Ann Arbor
  • PhD University of Chicago
  • Postdoctoral training: University of Georgia, Athens
Patel, S., E. Vierling, F. Tama. Replica exchange molecular dynamics simulations provide insight into substrate recognition by small heat shock proteins. Biophys. J. 106:2644-2655 (2014).
Xu, S., D. Guerra, U. Lee, E. Vierling. S-Nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis. Front. Plant Sci., 4: 1-13 (2013). doi: 10.3389/fpls.2013.00430
Basha, E. C. Jones, A.E. Blackwell, G. Cheng, E.R. Waters, K.A. Samsel*, M. Siddique, V. Pett, V. Wysocki, E. Vierling. An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones. J. Mol. Biol. 425:1683-96. PMID: 23416558 PMCID: PMC3646915 (2013).
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, 24:3349-65 (2012). PMID: 22942382 PMCID: PMC3462636
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).
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).
Contact Info

Department of Biochemistry and Molecular Biology
Life Science Laboratories N329
240 Thatcher Way
Amherst, MA 01003-9292

(413) 577-2890