TI  - Cross-family dimerization of transcription factors  <prot>Fos</prot> / <prot>Jun</prot>  and  <prot>ATF</prot> / <prot>CREB</prot> 
      alters DNA binding specificity.
PG  - 3720-4
AB  - The  <prot>Fos</prot> / <prot>Jun</prot>  and  <prot>ATF</prot> / <prot>CREB</prot>  families of transcription factors function in
      coupling extracellular signals to alterations in expression of specific
      target genes. Like many eukaryotic transcription factors, these proteins
      bind to DNA as dimers. Dimerization is mediated by a structure known as
      the &quot;leucine-zipper&quot; motif. Although  <prot>Fos</prot> / <prot>Jun</prot>  and  <prot>ATF</prot> / <prot>CREB</prot>  were previously
      thought to interact preferentially with different DNA regulatory elements
      (the AP-1/TRE and ATF/CRE sites, respectively), we find that members of
      these two families form selective cross-family heterodimers. The resulting
      heterodimers display distinguishable DNA binding specificities from each
      other and from their parental homodimers. These findings indicate that the
       <prot>Fos</prot> / <prot>Jun</prot>  and  <prot>ATF</prot> / <prot>CREB</prot>  families of transcription factors are not as distinct
      as was previously thought. We suggest that they can be grouped into a
      superfamily of transcription factors.
AD  - Department of Medical Biochemistry, Ohio State University, Columbus 43210.
