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A New Twist on Twist

The Twist1 transcription factor, a regulator in development and a key factor in tumorigenesis, is a known transcription inhibitor. It functions by binding to the E-box DNA consensus sequence. Twist has also been shown to be involved in transcriptional activation, but the mechanism for this activity is unknown.

The Twist1 transactivation domain is likely to adopt an -helical structure.

In this Paper of the Week, Kristian Bruun Laursen and colleagues show that heterodimeric complexes of Twist1 and transcription factor E12 mediate E-box-dependent transcriptional activation. They also identify a novel Twist1 transactivation domain, which functions independently of and more potently than the E12 activation domain. Finally, they have found three specific residues essential for the transactivating function of murine Twist1 and suggest an -helical structure of the transactivation domain.

Although it is not surprising that a known repressor of DNA activation can also be an activator, the multiple effects of Twist1 have been perplexing, and this paper contributes to our understanding of the several ways in which Twist can interact with DNA.

FOOTNOTES

See referenced article, J. Biol. Chem. 2007, 282, 34623-34633

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