Structural insights into TAZ2 domain–mediated CBP/p300 recruitment by transactivation domain 1 of the lymphopoietic transcription factor E2A
Marina Lochhead, Alexandra D. Brown, Alyssa C. Kirlin, Seth Chitayat, Kim Munro, Jane E. Findlay, George S. Baillie, David P. LeBrun, David N. Langelaan, Steven P. Smith
Abstract
ΦΦ motif to bind TAZ2. Whereas this region overlapped with the KIX recognition region, key KIX-interacting E2A-AD1 residues were exposed, suggesting that E2A-AD1 could simultaneously bind both the KIX and TAZ2 domains. However, we did not detect a ternary complex involving E2A-AD1, KIX, and TAZ2 and found that E2A containing both intact AD1 and AD2 is required to bind to CBP/p300. Our findings highlight the structural plasticity and promiscuity of E2A-AD1 and suggest that E2A binds both the TAZ2 and KIX domains of CBP/p300 through AD1 and AD2.
Topics & Concepts
TransactivationCREB-binding proteinTranscription factorBiologyCell biologyTranscription (linguistics)Protein–protein interactionTernary complexHEK 293 cellsPlasma protein bindingMolecular biologyGeneticsCREBGeneBiochemistryPhilosophyLinguisticsEnzymeCancer-related gene regulationImmune Cell Function and InteractionProtein Degradation and Inhibitors