spaceprovided)The goal of this research is to reveal the molecular composition and functions of the 26S proteasome in amulticellular eukaryote, using Arabidopsis thaliana as the model. Organisms rely on protein degradation fora variety of essential functions, including the maintenance of free amino acid pools, the removal of damagedproteins, and the control of regulatory protein abundance. The major machine for this breakdown is the 26Sproteasome, an ATP-dependent 2-MDa proteolytic complex.
The specific aim of this project is to define thecomposition of the native 26S proteasome from Arabidopsis, reveal the functions of various subunits, anddetermine whether the plant preferentially assembles specific subtypes of the complex through selectivepairing of various isoforms. A more complete characterization of the 26S proteasome will lead to a deeperunderstanding of how proteins are selectively degraded which may potentially identify new ways to controlprotein breakdown in vivo. Given the importance of Ub and the 26S proteasome to almost all facets ofeukaryotic physiology and development, this work should have practical benefits to both medicine andagriculture, including various disease caused by defects in the Ubiquitin/26S proteasome system.

Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31NS054563-04
Application #
7544940
Study Section
Special Emphasis Panel (ZRG1-F05 (20))
Program Officer
Sutherland, Margaret L
Project Start
2006-01-01
Project End
2009-12-16
Budget Start
2009-01-01
Budget End
2009-12-16
Support Year
4
Fiscal Year
2009
Total Cost
$20,130
Indirect Cost
Name
University of Wisconsin Madison
Department
Genetics
Type
Schools of Earth Sciences/Natur
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715