Professor Microbiology & Molecular Genetics, Medical School
Development Program Director New Investigator Development Program, Medical School
President GSBS Faculty
Education & Training
- Postdoctoral Fellow
- University of Michigan
- University of California-Davis, 1996
Areas of Interests
- Research Interest
- Protein chaperones and stress response in Saccharomyces cerevisiae
Protein chaperones and stress response in Saccharomyces cerevisiae
The heat shock response is highly conserved in all kingdoms, making it one of the most ancient cellular regulatory systems.
We have two primary interests:
- how heat shock is sensed and transduced to yield a genome-wide transcriptional response
- how protein chaperones, including the Hsp70, Hsp90 and the Hsp110 groups, function collaboratively within the cell during normal growth and during adaptation to environmental stress
The baker’s yeast, Saccharomyces cerevisiae, is an ideal microbial model system in which to investigate these questions, due to its facile genetics, genomics and ease of manipulation. These studies will directly impact our understanding of how human cells respond to pathophysiological states such as cancer and anoxia which strongly induce a heat shock response. In addition, there is growing evidence that the amyloid diseases of protein misfolding, including prion-based maladies such as Creutzfelt-Jakob (mad cow), and other triplet-repeat type diseases including Alzheimer’s, Parkinson’s, and Huntington’s, are intimately linked to protein chaperone expression and function.
- Verghese, J., Abrams, J., Wang, Y. and Morano KA (2012) Biology of the heat shock response and protein chaperone: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol. Mol. Biol. Rev. In Press.
- Morano KA, Grant, CM and Moye-Rowley, WS. (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics. 190:1157-1195.
- West, JD, Stamm CE, Brown HA, Justice SL and Morano KA (2011) Enhanced toxicity of the protein cross-linkers divinyl sulfone and diethyl acetylenedicarboxylate in comparison to related monofunctional electrophiles. Chem. Res. Toxicol. 24:1457-1459.
- Mandal AK, Gibney PA, Nillegoda, NB, Theodoraki MA, Caplan AJ and Morano KA (2010) Hsp110 chaperones control client fate determination in the Hsp70/Hsp90 chaperone system. Mol. Biol. Cell 21:1439-1448.
- Tapia H and Morano KA (2010) Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol. Biol. Cell 21: 63-72.
- Trott A West JD, Klaic L, Westerheide SD, Silverman RB, Morimoto RI and Morano KA (2008) Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thiol-targeted molecule. Mol Biol Cell 19:1104-1112.
- Shaner L, Gibney PA and Morano KA (2008) The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis. Curr Genet 54:1-11.
- Schuermann JP, Jiang J, Cuellar J, Llorca O, Wang L, Gimenez LE, Jin S, Taylor AB, Demeler B, Morano KA, Hart PJ, Valpuesta JM, Lafer EM and Sousa R. (2008) Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol Cell 31:232-243.
- Gibney PA, Fries T, Bailer SM and Morano KA (2008) Rtr1 is the Saccharomyces cerevisiae homolog of a novel family of RNA polymerase II-binding proteins. Eukaryot Cell 7:938-948.
- Shaner L and Morano KA (2007) All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity. Cell Stress Chaperones 12:1-8.
- Fan Q, Park KW, Du Z, Morano KA and Li L (2007) The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. Genetics 177:1583-1593.
- Shaner L, Sousa R, and Morano KA (2006) Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 45:15075-15084.