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Structure-function study on Rpn10 monoubiquitination

AuthorsPuig-Sàrries, Pilar
AdvisorCrosas, Bernat
Issue Date18-Jun-2015
PublisherCSIC - Instituto de Biología Molecular de Barcelona (IBMB)
Universitat Ramón Llull
AbstractCellular homeostasis depends, partially, on the proteolysis regulated by the Ubiquitin-Proteasome System (UPS). This proteolysis includes the degradation of misfolded, damaged or unnecessary proteins for the cell and comprises two phases. In the first stage, molecules of Ubiquitin are attached covalently to a target substrate at the amide group (ε-NH2) of some lysine residues. This process depends on the enzymatic activity of three enzymes, E1, E2 and E3. Afterwards, the proteasome takes care of the degradation of the substrate. The proteasome is a barrel-shaped multiprotein complex of 2,5 MDa present in the nucleus and cytosol of eukaryotic and Archaebacteria cells. The canonical degradation signal is a chain of ubiquitins, which is built via isopeptide bonds between the glycine G76 at the C-terminus of the molecule and lysine K48 of the next Ubiquitin.
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