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Cloning and characterization of a novel splicing isoform of USF1.

Authors :
Saito T
Oishi T
Yanai K
Shimamoto Y
Fukamizu A
Source :
International journal of molecular medicine [Int J Mol Med] 2003 Aug; Vol. 12 (2), pp. 161-7.
Publication Year :
2003

Abstract

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.

Details

Language :
English
ISSN :
1107-3756
Volume :
12
Issue :
2
Database :
MEDLINE
Journal :
International journal of molecular medicine
Publication Type :
Academic Journal
Accession number :
12851711