Elizabeth Vierling

vierling@u.arizona.edu
www.biochem.arizona.edu/dept/ppl/Profiles/vierling.html

CV

Elizabeth Vierling received a B.S. in Botany from the University of Michigan in 1975 and a Ph.D. in Biology from the University of Chicago in 1982. She did postdoctoral research in Molecular Biology at the University of Georgia. Here at the University of Arizona she teaches undergraduate Biochemistry for majors and Core Concepts in Plant Biology for graduate students. Her current research interests are the understanding the biological roles of molecular chaperones in plant stress and development. The lab uses a wide range of biochemical, molecular and genetic approaches, including basic protein biochemistry, microarrays of gene expression, and forward and reverse genetics in Arabidopsis.

Research Interest

• Research in our laboratory is aimed at understanding the mechanism of action and biological roles of molecular chaperones/heat shock proteins, both during stress (primarily heat stress) and during normal growth and development. In addition, we have an expanding program to define factors other than chaperones that are essential for heat stress tolerance. Our research extends from protein structural studies to molecular and quantitative genetic analysis, and utilizes Arabidopsis thaliana, the cyanobacterium Synechocystis PCC6803, and the yeast Saccharomyces cerevisiae as model organisms. On the structural side our work is contributing to basic knowledge of chaperone structure and function, while at the level of the whole organism, we are unraveling stress responses and mechanisms of stress tolerance. These studies involve basic biochemistry as well as molecular and transmission genetics. We are also employing microarray genomic techniques and have active collaborations in mass spectrometry and crystallography.
• One class of chaperones that are the subject of major research effort is the alpha-crystallin related small (s) HSPs. In vitro, sHSPs act as molecular chaperones to prevent the irreversible heat-denaturation of other proteins. In vivo, mutations in these proteins in mammals are responsible for certain types of myopathies as well as cataract formation. sHsps also accumulate in specific cancers and in neurodegenerative disease. We are pursuing both biochemical and genetic approaches to investigate further the function and mechanism of chaperone activity of the sHSPs through protein purification and in vitro assays of chaperone activity, as well as genetic analysis to identify and characterize sHsp mutants.
• To define other genes involved in stress tolerance, we have a program of both forward and reverse genetics and gene microarray experiments. Using a forward genetic screen for loss-of- thermotolerance we have identified mutants in another class of chaperones important to plants, Hsp101, a member of the AAA+ family of ATPases, which appears to be involved in disassociating protein aggregates accumulated during stress. Other mutants uncovered in this screen are being investigated. By probing Arabidopsis whole genome microarrays we have identified genes associated with acclimation to high temperature, and are now testing their importance using loss-of-function mutants.

Selected Publications

1. Giese, K.C., Basha, E., Catague, B.Y. and Vierling, E. (2005) Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity. Proc. Natl. Acad. Sci. USA 102, 18896-18901.
2. Lee, U., Wie, C., Escobar, M., Williams, B., Hong, S.-W. and Vierling, E. (2005) Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the sHsp chaperone system. Plant Cell 17, 559-571.
3. Giese,K.C. and E. Vierling. Mutants in a small heat shock proteins that affect the oligomeric state: analysis and allele specific suppression. J.
   Biol. Chem. 279: 32674 - 32683 (2004).
4. Lum, R., J. M. Tkach, E. Vierling, and J. R. Glover. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279: 29139 - 29146 (2004).
5. Basha, E., G. J. Lee, L. A. Breci, A.C. Hausrath, N. R. Buan, K C. Giese and E. Vierling. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates these chaperones protect a wide range of cellular functions. J. Biol. Chem., 279: 7566-7575 (2004).
6. Friedrich, K. L., K. C. Giese, N. R. Buan, and E. Vierling. Interactions between small heat shock protein subunits and substrate in small heat shock protein/substrate complexes. J. Biol. Chem. 279:1080-1089 (2004).