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Echinobase
ECB-ART-31108
Gene Expr 1992 Jan 01;23:231-40.
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Members of the USF family of helix-loop-helix proteins bind DNA as homo- as well as heterodimers.

Sirito M , Walker S , Lin Q , Kozlowski MT , Klein WH , Sawadogo M .


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We have isolated human cDNA clones for USF2, a new member of the upstream stimulatory factor (USF) family of transcription factors. Analysis of these clones revealed the existence of highly conserved elements in the C terminal region of all USF proteins. These include the basic region, helix-loop-helix (HLH) motif, and, in the case of the human proteins, the C-terminal leucine repeat (LR). In addition, a highly conserved USF-specific domain is located immediately upstream of the basic region. Using in vitro translated proteins, we found that all members of the USF family bound DNA as dimers. The N-terminal portion of USF, including the USF-specific domain, was entirely dispensable for dimer formation and DNA-binding. However, deletion mutants of USF2 lacking the LR were deficient in DNA-binding activity. Interestingly, each of the USF proteins could form functional heterodimers with the other family members, including the sea urchin USF, which does not have a LR motif. This indicates that the conserved LR in human USF is not required for dimer formation, and influences only indirectly DNA-binding.

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Genes referenced: LOC100887844 usf2

References [+] :
Beckmann, The leucine zipper of TFE3 dictates helix-loop-helix dimerization specificity. 1991, Pubmed