Processing of the cysteine protease aleurain
EMSL Project ID
2503
Abstract
This is a project funded by my DOE grant (DE-FG03-97ER20277) from the Office of Energy Biosciences. We are purifying a protease that is localized in a specific prevacuolar compartment in plant cells. This protease cleaves the proenzyme for aleurain (an aminopeptidase) to activate it. Active aleurain is then deposited in a vacuole where it presumably helps degrade proteins. Aleurain appears to be an essential enzyme because if you make too much of it or if you don't make any of it you die (if you are a tobacco plant). We now have the processing enzyme substantially purified although there are still perhaps 12 protein bands in our active fraction. We need to do tryptic digests on bands cut from SDS gels and identify the peptides. The source of the protein is cauliflower, which is a relative of Arabidopsis. This fact makes it more likely we will be able to in fact identify the proper peptides and an ortholog in the Arabidopsis genome.
Project Details
Project type
Exploratory Research
Start Date
2003-03-11
End Date
2003-08-05
Status
Closed
Released Data Link
Team
Principal Investigator