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Activation domains of stably bound GAL4 derivatives alleviate repression of promoters by nucleosomes.

Abstract：

:GAL4 derivatives containing an activation domain alleviated repression of a promoter during nucleosome assembly. A GAL4 derivative lacking an activation domain stably bound the promoter during nucleosome assembly but was not sufficient to preserve promoter function. The activation domain of GAL4 derivatives was essential for preserving promoter function, and thus the transcriptional stimulatory activity attributable to these activation domains increased dramatically during nucleosome assembly. Furthermore, promoter-bound activation domains allowed the formation of preinitiation complexes after nucleosome assembly. Finally, GAL4 derivatives containing activation domains significantly stimulated transcription through bacterially produced yeast TFIID only from nucleosome-assembled templates. These data indicate that acidic activation domains stimulate transcription by enhancing the ability of basal transcription factors to compete with nucleosomes for occupancy of the promoter.

journal_name

Cell

journal_title

Cell

authors

Workman JL,Taylor IC,Kingston RE

doi

10.1016/0092-8674(91)90237-s

subject

Has Abstract

pub_date

1991-02-08 00:00:00

pages

533-44

issue

3

eissn

0092-8674

issn

1097-4172

pii

0092-8674(91)90237-S

journal_volume

64

pub_type

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