We have been studying the mechanism of substrate recognition by the ubiquitin/proteasome pathway. We previously identified the yeast G-alpha protein as a target of the N-end rule pathway; a specific substrate-targeting mechanism of the ubiquitin system. G-alpha is a regulator of the mating response to yeast, and is functionally similar to its mammalian counterparts. We recently published a paper describing the isolation and detailed characterization of a degradation signal to G-alpha. Overexpression of the N-end rule pathway causes growth arrest in yeast cells. We isolated Rad23 as a suppressor of this toxicity. Rad23 was previously identified as a factor that is required for nucleotide excision repair in yeast and humans. We have recently reported that both yeast and human Rad23 3 proteins can form stable interactions with catalytically active proteasomes. Current experiments are designed to determine the sequences and conditions that mediate Rad23/proteasome interaction. We are also investigating the significance of phosphorylation in rad23 function. These studies form a major new direction in our laboratory.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
1F31GM020274-01
Application #
6016604
Study Section
Minority Programs Review Committee (MPRC)
Project Start
2000-02-28
Project End
Budget Start
2000-02-28
Budget End
2001-02-27
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost
Name
University of Medicine & Dentistry of NJ
Department
Biochemistry
Type
Schools of Medicine
DUNS #
622146454
City
Piscataway
State
NJ
Country
United States
Zip Code
08854