T. Davissmyth et al., THE FAR UPSTREAM ELEMENT-BINDING PROTEINS COMPRISE AN ANCIENT FAMILY OF SINGLE-STRAND DNA-BINDING TRANSACTIVATORS, The Journal of biological chemistry, 271(49), 1996, pp. 31679-31687
The cloning and expression of two new human cDNAs encoding proteins hi
ghly related to the far upstream element-binding protein (FBP) are des
cribed, FBP, FBP2, and FBP3 comprise a family of single-strand DNA-bin
ding proteins that possess all of the general features of more convent
ional transcription factors. The FBPs each bind sequence specifically
to only one strand of the far upstream element (FUSE; originally ident
ified upstream of c-myc), and each possesses potent activation domains
when fused to the GAL4 DNA-binding domain and assayed by transient tr
ansfection. Typical of transcription factors, the proteins are most hi
ghly related in their central, DNA-binding domains, but extensive homo
logy is also shared within the tyrosine-rich, carboxyl-terminal activa
tion domains. Comparison with Gen Bank sequences revealed a fourth FBP
family member encoded by Caenorhabditis elegans chromosome III, illus
trating the high degree of homology in this evolutionarily ancient and
conserved family.