Identification of a Novel SNF2/SWI2 Protein Family Member, SRCAP, Which Interacts with CREB-binding Protein*

Abstract

The ability of cAMP response-element binding protein (CREB)-binding protein (CBP) to function as a co-activator for a number of transcription factors appears to be mediated by its ability to act as a histone acetyltransferase and through its interaction with a number of other proteins (general transcription factors, histone acetyltransferases, and other co-activators). Here we report that CBP also interacts with a novel ATPase termedSnf2-Related CBPActivator Protein (SRCAP). Consistent with this activity, SRCAP contains the conserved ATPase domain found within members of the Snf2 family. Transfection experiments demonstrate that SRCAP is able to activate transcription when expressed as a Gal-SRCAP chimera and that SRCAP also enhances the ability of CBP to activate transcription. The adenoviral protein E1A was found to disrupt interaction between SRCAP and CBP possibly representing a mechanism for E1A-mediated transcriptional repression.

Footnotes

  • * The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

    The nucleotide sequence(s) reported in this paper has been submitted to the GenBank™/EMBL Data Bank with accession number(s)  AF143946.

  • § The first two authors contributed equally to this work.

  • To whom correspondence should be addressed. Tel.: 314-268-5291; Fax: 314-577-8233; E-mail: Chrivia{at}SLU.edu.

  • Abbreviations:
    CREB

    cAMP response-element binding protein

    CBP

    CREB-binding protein

    NCoA

    nuclear receptor coactivator

    P/CAF

    p300/CBP associated factor

    SRCAP

    Snf2-Related CBPActivator Protein

    PCR

    polymerase chain reaction

    kb

    kilobase(s)

    • Received December 8, 1998.
    • Revision received March 16, 1999.
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