My 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.
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Quaternary Dynamics and Plasticity Underlie Small Heat Shock Protein Chaperone Function (with Andrew J. Baldwin, Alexander J. Painter, Nomalie Jaya, Eman Basha, Lewis E. Kay, Carol V. Robinson, and Justin L. P. Benesch), Proceedings of the National Academy of Sciences (2009)
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that prevent protein...
Substrate Binding Site Flexibility of the Small Heat Shock Protein Molecular Chaperones (with Victor Garcia), Proceedings of the National Academy of Sciences (2009)
Small heat shock proteins (sHSPs) serve as a first line of defense against stress-induced cell...
Insights Into Small Heat Shock Protein and Substrate Structure During Chaperone Action Derived from Hydrogen/Deuterium Exchange and Mass Spectrometry. (with Eman Basha and Vicki H. Wysocki), Journal of Biological Chemistry (2008)
Small heat shock proteins (sHSPs) and the related alpha-crystallins are ubiquitous chaperones linked to neurodegenerative...
Heat Shock Protein 101 Effects in A. Thaliana: Genetic Variation, Fitness and Pleiotropy in Controlled Temperature Conditions. (with C. Scott and I. Boumaza), Molecular Ecology (2008)
The Hsp100/ClpB heat shock protein family is ancient and required for high temperature survival, but...
Modulation of Nitrosative Stress by S-Nitrosoglutathione Reductase is Critical for Thermotolerance and Plant Growth in Arabidopsis (with Chris Wie, Bernadette O. Fernandez, and Martin Feelisch), Plant Cell (2008)
Nitric oxide (NO) is a key signaling molecule in plants. This analysis of Arabidopsis thaliana...