A B C D E F G H J K L M N O P R S T V W X Y Z

Please select the first letter of the last name you are looking for.

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 sites.biochem.umass.edu/vierlinglab/

Academic Background:

  • BS University of Michigan, Ann Arbor
  • PhD University of Chicago
  • Postdoctoral training: University of Georgia, Athens
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. in press (2018).
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 & Chap. https://doi.org/10.1007/s12192-018-0884-3 (2018).
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).
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).
Zhang, L. X. Liu, K. Gaikwad, X. Kou, F. Wang, X. Tian, M. Xin, Z. Ni, Q. Sun, H. Peng, E. Vierling. Mutations in eIF5B confer thermosensitive and pleiotropic phenotypes via translation defects in Arabidopsis thaliana. Plant Cell. 29:1952-1969 (2017). Kim, M., F. McLoughlin, E. Basha, E. Vierling. Assessing tolerance to acute heat stress. Bio-protocol 7(14): e2405. DOI: 10.21769/BioProtoc.2405 (2017).
McLoughlin, F., E. Basha, M. E. Fowler*, M. Kim, J. Bordowitz*, S. Katiyar-Agarwal, E. Vierling. Class I and II small heat shock proteins together with HSP101 protect eukaryotic protein translation factors during heat stress. Plant Physiol. 172:1221-1236 (2016).
Guerra, D., K. Ballard, I. Truebridge*, E. Vierling. S-nitrosation of conserved cysteines modulates activity and stability of S-nitrosoglutathione reductase (GSNOR). Biochemistry 55:2452-64 (2016).
 
Contact Info

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

(413) 577-2890
vierling@biochem.umass.edu

sites.biochem.umass.edu/vierlinglab/

Seal of The University of Massachusetts Amherst - 1863
©2024 University of Massachusetts Amherst · Site Policies · Accessibility