This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Protein ubiquitination and degradation plays a key role in many cellular events, including cell cycle control, the stress response, differentiation, circadian rhythms, signal transduction, metabolic control and DNA damage repair. The ubiquitination and proteosomal protein degradation machinery are highly conserved in eukaryotic cells. With 8xHis-tagged ubiquitin, we are now capable of selectively enriching ubiquitinated proteins in budding yeast S. cerevisiae. Using purified isotope labeled proteins as internal standards, combined with capillary peptide liquid chromatography and tandem mass spectrometry, we are trying to quantitatively determine the ubiquitinated protein level in oxidative DNA damage condition. DNA damage induced by reactive oxygen species (ROS) is an important intermediate in the pathogenesis of human conditions such as cancer and aging. We believe that quantitative measurement of ubiquitinated protein level would help to advance significantly the contribution of proteomics to the development of novel therapeutics.
Showing the most recent 10 out of 583 publications
