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J Biol Chem. 2001 Oct 26;276(43):40127-32. Epub 2001 Aug 20.

How transcriptional activators bind target proteins.

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  • 1Department of Natural Sciences, Södertörns högskola, Box 4101, S-14104 Huddinge, Sweden. Stefan.Hermann@sh.se


The product of the proto-oncogene c-myc influences many cellular processes through the regulation of specific target genes. Through its transactivation domain (TAD), c-Myc protein interacts with several transcription factors, including TATA-binding protein (TBP). We present data that suggest that in contrast to some other transcriptional activators, an extended length of the c-Myc TAD is required for its binding to TBP. Our data also show that this interaction is a multistep process, in which a rapidly forming low affinity complex slowly converts to a more stable form. The initial complex formation results from ionic or polar interactions, whereas the slow conversion to a more stable form is hydrophobic in nature. Based on our results, we suggest two alternative models for activation domain/target protein interactions, which together provide a single universal paradigm for understanding activator-target factor interactions.

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