| Name: |
| Jill L. Johnson |
| Title: |
| Assistant Professor |
| Degree: |
| Ph.D., 1994, Mayo Graduate School, Rochester, MN |
| Phone: |
| (208) 885-9767 |
| Fax: |
| (208) 885-6518 |
| Email: |
| jilljohn@uidaho.edu |
| Lab/Office Location: |
| Gibb Hall, Room 120 |
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| Research Interests: |
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My research focuses on the role of molecular chaperones in the cell. Molecular chaperones are highly conserved proteins found in
every cellular compartment of every organism studied. In general, chaperones prevent inappropriate interactions that may result in
proteins becoming unfolded, and they function both during normal cellular processes, such as protein synthesis, and also during
times of environmental stress, such as heat shock.
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In particular, I study the function of a chaperone called Hsp90 (90 kDa heat shock protein). Hsp90 is an essential chaperone that is
required for the activity of a number of 'client' proteins involved in signal transduction pathways and cell cycle regulation, such
as steroid hormone receptors and oncogenic tyrosine kinases. Hsp90 functions with at least 5 other proteins in an ordered pathway of
interaction that results in the proper folding and activity of the client protein. I use genetic and biochemical studies with the
yeast, Saccharomyces cerevisiae, in an attempt to understand what all these co-chaperones are doing and why so many of them
are required. My current work focuses on the role of two of these co-chaperones, Hsp40 and Hsp70, which interact with client
proteins before Hsp90. I am interested in determining what structural features of a client protein promote interaction with Hsp40
and Hsp70, as well as investigating how Hsp90 is recruited to the pathway.
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| Selected Publications: |
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Johnson JL and Brown C. Plasticity of the Hsp90 molecular chaperone machine. (2008) Cell Stress and Chaperones. In press.
Flom G, Behal RH, Rosen L, Cole DG and Johnson JL. (2007) Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem. J. 404, 159-167.
Johnson JL, Halas A and Flom G. Nucleotide-dependent interaction of yeast Hsp90 with the cochaperone proteins Sti1, Sba1 and Cpr6. (2007) Molec. Cell. Biol. 27(2):768-776.
Flom G, Weekes J, Williams J, and Johnson JL. (2006) Effect of mutation of the TPR and DP2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. In press. Genetics. 172(1):41-51.
Flom G, Weekes J and Johnson JL. (2005). Novel interaction of the Hsp90 molecular chaperone machine with Ssl2, and essential DNA helicase in Saccharomyces cerevisiae. Current Genetics. 47:368-380.
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