A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein.

Abstract:

:Biochemical and genetic studies suggest the existence of mediators that work between the activation domains (ADs) of regulatory proteins and the basic transcriptional machinery. We have previously shown genetically that Sug1 interacts with the AD of the yeast activator Ga14. Here we provide evidence that the Sug1 protein of yeast binds directly to the ADs of Ga14 and the viral activator, VP16. Sug1 protein is associated with the TATA-binding protein in vivo and binds to it in vitro, consistent with a mediator function. We also demonstrate that Sug1 is not a component of the 26S proteasome, contrary to previous reports. Sug1 is a member of a large, highly conserved family of ATPases, implying a role for ATP hydrolysis in the activation of transcription.

journal_name

Nature

journal_title

Nature

authors

Swaffield JC,Melcher K,Johnston SA

doi

10.1038/374088a0

subject

Has Abstract

pub_date

1995-03-02 00:00:00

pages

88-91

issue

6517

eissn

0028-0836

issn

1476-4687

journal_volume

374

pub_type

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