The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair protein Rad23

摘要: Yeast peptide: N-glycanase (PNGase) is involved in the proteasomal degradation of misfolded glycoproteins where it interacts with DNA repair protein Rad23 as first detected a yeast two-hybrid assay and subsequently confirmed by biochemical vivo analyses. Limited proteolysis PNGase trypsin led to removal both an N-terminal C-terminal stretch. Based on these truncations region was identified being responsible for binding Rad23. Secondary structure predictions this suggest that composed single, solvent-exposed alpha-helix. The interaction between studied using surface plasmon resonance revealing equilibrium constant approximately 2.5 microM. oligomeric nature also investigated sedimentation analysis. Although exists dimer solution, monomeric form associates monomer 1:1 stoichiometric ratio.