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GAL4-VP16 is an unusually potent transcriptional activator

Nature volume 335, pages 563–564 (1988)Cite this article

Abstract

Recent work has defined a class of transcriptional activators1–5, members of which activate transcription in yeast, plant, insect and mammalian cells6–9. These proteins contain two parts: one directs DNA binding and the other, called the activating region, presumably interacts with some component of the transcriptional machinery. Activating regions are typically acidic and require some poorly-understood aspect of structure, probably at least in part an α-helix1–5,10. Here we describe a new member of this class, formed by fusing a DNA-binding fragment of the yeast activator GAL4 to a highly acidic portion of the herpes simplex virus protein VP16 (ref. 11; also called Vmw65). VP16 activates transcription of immediate early viral genes by using its amino-terminal sequences to attach to one or more host-encoded proteins that recognise DNA sequences in their promoters11–15. We show that the hybrid protein (GAL4-VP16) activates transcription unusually efficiently in mammalian cells when bound close to, or at large distances from the gene. We suggest that the activating region of VP16 may be near-maximally potent and that it is not coincidental that such a strong activator is encoded by a virus.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Ivan Sadowski, Jun Ma & Mark Ptashne

  2. Department of Biochemistry, Michigan State University, East Lansing, Michigan, 48824, USA

    Steve Triezenberg

Authors
  1. Ivan Sadowski
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  2. Jun Ma
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  3. Steve Triezenberg
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  4. Mark Ptashne
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Sadowski, I., Ma, J., Triezenberg, S. et al. GAL4-VP16 is an unusually potent transcriptional activator. Nature 335, 563–564 (1988). https://doi.org/10.1038/335563a0

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