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The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators.

Authors :
Davis-Smyth, T
Duncan, R C
Zheng, T
Michelotti, G
Levens, D
Source :
Journal of Biological Chemistry; December 1996, Vol. 271 Issue: 49 p31679-87, 9p
Publication Year :
1996

Abstract

The cloning and expression of two new human cDNAs encoding proteins highly related to the far upstream element-binding protein (FBP) are described. FBP, FBP2, and FBP3 comprise a family of single-strand DNA- binding proteins that possess all of the general features of more conventional transcription factors. The FBPs each bind sequence specifically to only one strand of the far upstream element (FUSE; originally identified upstream of c-myc), and each possesses potent activation domains when fused to the GAL4 DNA-binding domain and assayed by transient transfection. Typical of transcription factors, the proteins are most highly related in their central, DNA-binding domains, but extensive homology is also shared within the tyrosine-rich, carboxyl-terminal activation domains. Comparison with GenBank sequences revealed a fourth FBP family member encoded by Caenorhabditis elegans chromosome III, illustrating the high degree of homology in this evolutionarily ancient and conserved family.

Details

Language :
English
ISSN :
00219258 and 1083351X
Volume :
271
Issue :
49
Database :
Supplemental Index
Journal :
Journal of Biological Chemistry
Publication Type :
Periodical
Accession number :
ejs7198136