GAL4-VP16 is an unusually potent transcriptional activator.

Abstract:

:Recent work has defined a class of transcriptional activators, members of which activate transcription in yeast, plant, insect and mammalian cells. 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 alpha-helix. 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 promoters. 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.

journal_name

Nature

journal_title

Nature

authors

Sadowski I,Ma J,Triezenberg S,Ptashne M

doi

10.1038/335563a0

subject

Has Abstract

pub_date

1988-10-06 00:00:00

pages

563-4

issue

6190

eissn

0028-0836

issn

1476-4687

journal_volume

335

pub_type

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