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1: Biochem Biophys Res Commun. 1997 Feb 13;231(2):333-9.Click here to read Links
Erratum in:
Biochem Biophys Res Commun 1997 Apr 7;233(1):293.

USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its bHLH domain and inhibits c-Maf DNA binding activity.

Kurschner C, Morgan JI.

Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

In screening for proteins that interact with the basic zipper (bZip) transcription factor, c-Maf, we isolated USF2/FIP. USF2 is a member of the bHLH-Zip protein family, possessing a basic (b) DNA binding region, a helix-loop-helix (HLH) motif, and a leucine zipper (Zip) structure. Mutants of USF2 that lacked a Zip formed heterodimers with c-Maf, but did not homodimerize. Deletion of the USF2 basic region or mutation of its helices abrogated its binding to c-Maf, but had no effect on homodimerization. A functional c-Maf bZip motif was necessary for both homodimerization and heterodimerization with USF2. These data suggest a tetrameric configuration for Maf-USF2 complexes. In the presence of USF2, the DNA binding activity of c-Maf was markedly reduced. Therefore, USF2 and c-Maf may interact to regulate gene expression.

PMID: 9070273 [PubMed - indexed for MEDLINE]