Participating Faculty
Jill Johnson
Name:Jill Johnson
Department:Biological Sciences
Credentials:1994 - Ph.D., Mayo Graduate School, Rochester MN
Office:Life Sciences South, Room 148
Mailing Address:

Biological Sciences
875 Perimeter Dr. MS 3051
Moscow, ID. 83844-3051

Research Interests

Molecular Chaperones

Research Summary

My laboratory is interested in the roles of molecular chaperones in regulating signal transduction pathways. In particular, we study the function of the cytosolic chaperone Hsp90, which interacts with a diverse subset of client proteins, ranging from steroid hormone receptors to protein kinases. Hsp90, along with a number of co-chaperone proteins, interacts with client proteins in an ordered, ATP-dependent pathway that is conserved from yeast to plants to humans. We use a combined genetic and biochemical approach in Saccharomyces cerevisiae to dissect the individual roles of the co-chaperones in this folding pathway. Current work focuses establishing unique functions of the 12 Hsp90 co-chaperones in yeast.  This includes the potential role of Cpr6 in targeting clients to Hsp90, and the role of Cpr7 in mediating Hsp90 conformational changes.  Additional work focuses on the role of Hsp90 and co-chaperones in regulating the function and folding of Utp21, a protein required for ribosome biogenesis. By using both heterologous and native client proteins we hope to better understand how the Hsp90 molecular chaperone affects multiple cellular signaling pathways.

Research Publications

Zuehlke, A. D., et al. (2013). "Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis." J Biol Chem 288(38): 27406-27414.

Chiosis, G., et al. (2013). "A global view of Hsp90 functions." Nat Struct Mol Biol 20(1): 1-4.

Chiosis G, Dickey CA and Johnson J.L. (2013). A global view of Hsp90 functions. Meeting report. Nature Structural and Molecular Biology. 20 (1): 1-4.

Johnson J.L.(2012) Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim. Biophys Acta. 1823(3):607-13.

Flom GA, Langner E and Johnson J.L. (2012) Identification of an Hsp90 mutation that selectively disrupts cAMP/PKA signaling in Saccharomyces cerevisiae. Current Genetics 58(3):149-63.

Zuehlke A.D., and Johnson J.L. (2012). Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics. 191:805-814.

Cox MB and Johnson JL. (2011) The role of p23, Hop, immunophilins and other co-chaperones in regulating Hsp90 function. Methods and Protocols Series: Methods in Molecular Biology, Molecular Chaperones Vol. 787.  Chapter 4. Pages 45-66. Calderwood, Stuart K.; Prince, Thomas L. (Eds.), 2011, ISBN 978-1-61779-294-6

Zuehlke, A. and J. L. Johnson (2010). "Hsp90 and co-chaperones twist the functions of diverse client proteins." Biopolymers 93(3): 211-217.

Johnson J. L. and Brown C. Plasticity of the Hsp90 molecular chaperone machine in divergent  eukaryotic organisms. Cell Stress and Chaperones. 2009. 14:83-94.

Flom, G.A., M. Lemieszek, E.A. Fortunato, and J.L. Johnson, Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins. Mol Biol Cell, 2008. 19(12): p. 5249-58

Flom, G., R.H. Behal, L. Rosen, D.G. Cole, and J.L. Johnson, Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem J, 2007. 404(1): p. 159-67.

Johnson, J.L., A. Halas, and G. Flom, Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol Cell Biol, 2007. 27(2): p. 768-76.

Washington State University