Vierling studies molecular chaperones (a diverse group of proteins that assist in protein folding, transport, modulation, and regulation) and the processes that affect plant stress tolerance. She and her research group have focused their investigations on how two classes of molecular chaperones, the Hsp100/ClpB proteins and the small heat shock proteins (sHSPs), function in higher plants.
Small heat shock proteins are critical components of the cellular “protein quality control network” of molecular chaperones and enzymes that work to prevent the accumulation of abnormal or damaged proteins. Studies of sHSPs are relevant to human health because abated protein quality control often leads to diseased states and is associated with aging. Mutations in the related human proteins are responsible for eye cataracts, muscle myopathies, and neuropathies. Defining the mechanism of sHSP chaperone action has vast implications for understanding cellular stress and disease processes.
“Because they are capable of immediately binding unfolding proteins, sHSPs are the ‘first responders’ to cell stress. Understanding how sHSPs accomplish this feat is critical to defining their roles in protection of cells from stress,” says Vierling.
While much remains unknown about these environmental stresses and their associated impacts, Vierling’s work is showing that sHSPs may protect plants from heat stress. She and her colleagues have established that molecular chaperone Hsp101 is essential for plants to survive in high temperatures. Heat stress can severely limit crop productivity, particularly at critical stages of plant development.Vierling and her colleagues are also working with Synechocystis (pond scum) to further investigate these effects.
As a post-doctoral researcher in the 1980s, Vierling was part of a group that isolated genes connected to high-temperature stress response—research that formed the foundation for what scientists now refer to as ‘chaperones.’
“I started out working on how plant chloroplasts—the photosynthetic organelles of plants—respond to high temperature, and ended up discovering it involved chaperones,” Vierling explains.
Vierling has a well-established reputation in the field and is a Distinguished Professor at UMass Amherst. She was awarded a John Simon Guggenheim Memorial Fellowship in 2000, named a Fellow of the American Association for the Advancement of Science in 2002, received an Alexander von Humboldt Senior Research Fellowship in 2007, and in 2012 was named a Fellow of the American Society of Plant Biologists. Vierling’s work has been supported by the National Institutes of Health, the National Science Foundation, the Department of Energy, and the Department of Agriculture. Prior to coming to UMass Amherst in 2011, Vierling was a program director at the National Science Foundation (2008-2010) and a Regents’ Professor at the University of Arizona.
Vierling says that a strong biochemistry department, along with the state’s increasing support for the life sciences, brought her to UMass. She plans to continue her work on chaperone mechanisms, investigating precisely how they protect plants from stress, and looking more closely at how other proteins are connected with plant stress response.
“Elizabeth is considered a world leader in heat stress in plants…as a result, she’s a focal point for research both on and off campus,” says Jennifer Normanly, department head. “She gives generously of her time to university initiatives. She’s a wonderful colleague—a lovely addition to the department and to the campus.”
Amanda Drane '12
As a post-doctoral researcher in the 1980s, Elizabeth Vierling was part of a group that isolated genes connected to high-temperature stress response—research that formed the foundation for what scientists now refer to as ‘chaperones.’