This molecule first binds to an ATP-dependent E1 activating enzyme; it is then carried by an E2 convertase to its substrate, where it always forms a covalent bond to a lysine (LIE-seen) residue.
This molecule first binds to an ATP-dependent E1 activating enzyme; it is then carried by an E2 convertase to its substrate, where it always forms a covalent bond to a lysine (LIE-seen) residue. It was isolated independently in the mid-1970's by two groups, in Boston and Haifa; in 1980 Wilkinson et al. used rabbit cells to demonstrate that "ATP-dependent proteolysis factor 1" was the same protein as this well-known 76-amino acid protein. Not found in prokaryotes, it takes its name from its presence in all eukaryotic organisms in an extremely highly conserved form. Along with the proteasome, it is part of the UPS that is necessary for all energy-absorbing protein breakdown pathways. For ten points, what is this molecule, the study of which gleaned Irwin Rose, Aaron Ciechanover and Avram Herschko the 2004 Nobel Prize in Chemistry?
This molecule first binds to an ATP-dependent E1 activating enzyme; it is then carried by an E2 convertase to its substrate, where it always forms a covalent bond to a lysine (LIE-seen) residue.
{Ubiquitin}