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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Cloning and characterization of a novel splicing isoform of USF1.

The ubiquitous basic helix-loop-helix transcription factor USFs encoded by two distinct genes (USF1 and USF2) recognize a core motif, CACGTG, termed E box and regulate the expression of a variety of genes. USF1 and USF2 proteins form homo- and heterodimers to bind the target core motif DNA. Here, we report the molecular cloning and functional characterization of a novel alternative splicing variant of human USF1 (hUSF1), termed USF1/BD. Compared with USF1 wild-type (wt), USF1/BD lacks the N-terminal transactivation domain. Cloning and characterization of the hUSF1 genomic region revealed that USF1/BD is generated by excising the sequence corresponding to a part of exon 4. In transiently transfected cells, USF1/BD was localized in the nucleus and repressed the promoter activity of the human angiotensinogen gene. In vitro translated USF1/BD possessed DNA binding activity as a homodimer and a heterodimer with USF1 (wt). These results suggest that USF1/BD plays a role as a modulator of USF1 to control the expression of target genes.[1]

References

  1. Cloning and characterization of a novel splicing isoform of USF1. Saito, T., Oishi, T., Yanai, K., Shimamoto, Y., Fukamizu, A. Int. J. Mol. Med. (2003) [Pubmed]
 
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