Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation.

摘要: Hub proteins have central roles in regulating cellular processes. By targeting a single hub, viral oncogene may gain control over an entire module the interaction network that is potentially comprised of hundreds proteins. The adenovirus E1A oncoprotein hub interacts with many by short linear motifs/molecular recognition features (MoRFs). These interactions transform architecture protein and virtually reprogram cell. To identify additional MoRFs within E1A, we screened portions for their ability to activate yeast pseudohyphal growth or differentiation. This identified novel functional region conserved 2 sequence EVIDLT. MoRF necessary sufficient bind N-terminal SUMO conjugase UBC9, which also noncovalently involved polySUMOylation. Our results suggest interferes polySUMOylation, but not monoSUMOylation. data provide first insight into consequences was initially described 1996. We further demonstrate polySUMOylation regulates promyelocytic leukemia body reorganization E1A. In conclusion, UBC9 mimics normal binding between represents mechanism modulate