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. 1997 Jan;71(1):129–137. doi: 10.1128/jvi.71.1.129-137.1997

p300 family members associate with the carboxyl terminus of simian virus 40 large tumor antigen.

N L Lill 1, M J Tevethia 1, R Eckner 1, D M Livingston 1, N Modjtahedi 1
PMCID: PMC191032  PMID: 8985331

Abstract

Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s). The biological function of p400 is not yet known, but it is structurally and immunologically closely related to p300 and CREB-binding protein, two known E1A-binding transcription adapters. Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T). In anti-T coimmunoprecipitation experiments, staggered deletions spanning the amino-terminal 250 amino acids of T did not abrogate T binding to either p400 or p300. A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably. Anti-p53 immunoprecipitates prepared from cells containing wild-type T also contained p400 and p300. Hence, both p400 and p300 can bind (directly or indirectly) to a carboxyl-terminal fragment of T which contains its p53 binding domain. Since the p53 binding domain of T contributes to its immortalizing and transforming activities, T-p400 and/or T-p300 interactions may participate in these functions.

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Selected References

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