University of Idaho - I Banner
A student works at a computer

SlateConnect

U of I's web-based retention and advising tool provides an efficient way to guide and support students on their road to graduation. Login to SlateConnect.

Jill L. Johnson

Jill L. Johnson

Professor

Office

Life Sciences South 148

Phone

208-885-9767

Mailing Address

Dept. of Biological Sciences
University of Idaho
875 Perimeter MS 3051
Moscow, Idaho 83844-3051

Research: Cellular & Molecular Biology, Biochemistry

  • Ph.D. Biochemistry and Molecular Biology Mayo Graduate School, 1994
  • B.S. Cellular and Molecular Biology, University of Michigan, 1988

Research interests: Role of molecular chaperones in the cell, especially the study of a chaperone called Hsp90 (90 kDa heat shock protein).

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.

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.

Contact

Department of Biological Sciences

Physical Address:
Life Sciences South 252

Mailing Address:
875 Perimeter Drive MS 3051
Moscow, ID 83844-3051

Phone: 208-885-6280

Fax: 208-885-7905

Email: biosci@uidaho.edu

Web: Department of Biological Sciences