Gene-regulatory properties of Myc helix-loop-helix/leucine zipper mutants: Max-dependent DNA binding and transcriptional activation in yeast correlates with transforming capacity.

Journal article

Max is a basic helix-loop-helix/leucine zipper (bHLH/LZ) protein that forms sequence-specific DNA-binding complexes with the c-Myc oncoprotein (Myc). Using Saccharomyces cerevisiae, we have shown that the Max bHLH/LZ domain enables Myc to activate transcription through CACGTG and CACATG sequences in vivo, and that the number and context of such sites determines the level of activation. In addition, we have used yeast to investigate the role of the Myc helix-loop-helix (HLH) and leucine zipper...

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Authors: Crouch, D; Fisher, F; Clark, W; Jayaraman, P; Goding, C

• Publication status: Published
• Journal: Oncogene
• Volume: 8
• Issue: 7
• Pages: 1849-1855
• Publication date: 1993-07-01
• EISSN: 1476-5594
• ISSN: 0950-9232
• Language: English
• Keywords: Base Sequence; Transcription Factors; Leucine Zippers; Protein Structure, Secondary; DNA; Basic-Leucine Zipper Transcription Factors; Mutation; Molecular Sequence Data; Cell Transformation, Neoplastic; Saccharomyces cerevisiae; Transcriptional Activation; Proto-Oncogene Proteins c-myc; DNA-Binding Proteins