Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1998 Nov 6;273(45):29302-8.

Functional interactions of transcription factor human GA-binding protein subunits.

Author information

  • 1Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.

Abstract

The transcription factor human GA-binding protein (hGABP) is composed of two subunits, the Ets-related hGABPalpha, which binds to a specific DNA sequence, and either one of two hGABPalpha-associated subunits, hGABPbeta or hGABPgamma. The DNA-binding protein hGABPalpha cannot affect transcription by itself, but can modify hGABP-dependent transcription in vitro and in vivo in the presence of its associated subunits. In this study, co-transfection assays showed that the ratio of hGABPbeta to hGABPgamma affected transcription from a promoter containing hGABP binding sites. Biochemical analysis showed that they bind to hGABPalpha competitively, indicating that the ratio of hGABPbeta to hGABPgamma is important for hGABP complex formation. Kinetic analysis of the protein-protein interaction using the surface plasmon resonance system showed that hGABPalpha binds to hGABPbeta or hGABPgamma with similar equilibrium constants. Kinetic analysis of the DNA-hGABP interaction showed that the binding of hGABPgamma to hGABPalpha stabilized the interaction of hGABPalpha with its DNA binding site. In addition, the kinetic analysis revealed that this was due to a slower dissociation of the protein complex from the DNA. These results suggest that hGABPalpha-associated subunits influence the DNA binding stability of hGABPalpha and regulate hGABP-mediated transcription by competing with each other.

PMID:
9792629
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk