Human p300 protein is a cellular target of adenoviral E1A oncoprotein and a potential transcriptional coactivator. Both p300 and Rb family protein-binding regions of E1A are required for the repression of muscle gene expression, which is regulated by MyoD family transactivators, This implies that p300 is involved in MyoD-dependent transactivation, We show that the repression of MyoD mediated E box (MyoD consensus) reporter activity by E1A is correlated with its interaction with p300, indicating that p300 participates in MyoD-dependent transactivation, In addition, p300 is able to interact both in vivo and in vitro with MyoD through a portion at the carboxyl-terminal cysteine/histidine-rich domain and associates with the components of the basal transcriptional complex through its two separate transactivation domains at the amino and carboxyl termini, Consistent with its role as a coactivator, p300 potentiates MyoD-activated transcription.
Human p300 protein is a coactivator for the transcription factor MyoD
Caruso M;Felsani A;
1996
Abstract
Human p300 protein is a cellular target of adenoviral E1A oncoprotein and a potential transcriptional coactivator. Both p300 and Rb family protein-binding regions of E1A are required for the repression of muscle gene expression, which is regulated by MyoD family transactivators, This implies that p300 is involved in MyoD-dependent transactivation, We show that the repression of MyoD mediated E box (MyoD consensus) reporter activity by E1A is correlated with its interaction with p300, indicating that p300 participates in MyoD-dependent transactivation, In addition, p300 is able to interact both in vivo and in vitro with MyoD through a portion at the carboxyl-terminal cysteine/histidine-rich domain and associates with the components of the basal transcriptional complex through its two separate transactivation domains at the amino and carboxyl termini, Consistent with its role as a coactivator, p300 potentiates MyoD-activated transcription.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.