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Title: E-box variants direct formation of distinct complexes with the basic helix-loop-helix protein ALF1. Author: Bonven BJ, Nielsen AL, Nørby PL, Pedersen FS, Jørgensen P. Journal: J Mol Biol; 1995 Jun 09; 249(3):564-75. PubMed ID: 7783212. Abstract: The murine transcription factor ALF1 belongs to the class of basic helix-loop-helix proteins specific for the NCAGNTGN-version of the E-box. Binding of homodimeric ALF1 to variants of this motif was studied by a combination of binding site selection technology and DNA modification interference analysis. The results showed that substitutions at the non-conserved positions in the E-box sequence could cause profound alterations in the patterns of specific contacts at the protein-DNA interface. Thus, both the overall extent of the binding region and the backbone phosphate contact pattern differed markedly between closely related E-boxes with similar affinities for ALF1. The identity of the base at the inner N was an important determinant of contact pattern specification. The E-box variants differed in their ability to mediate ALF1 dependent transcriptional activation in vivo. We discuss the possibility that adaptability in basic helix-loop-helix protein-DNA interactions can result in complexes with different functional properties.[Abstract] [Full Text] [Related] [New Search]