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

Jonathan C. Swaffield, Karsten Melcher, Stephen Albert Johnston

Research output: Contribution to journalArticlepeer-review

130 Scopus citations

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 Sugl interacts with the AD of the yeast activator Ga141. Here we provide evidence that the Sugl protein of yeast binds directly to the ADs of Gal4 and the viral activator, VP16. Sugl 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 Sugl is not a component of the 26S proteasome, contrary to previous reports2-5. Sugl is a member of a large, highly conserved family of ATPases, implying a role for ATP hydrolysis in the activation of transcription.

Original languageEnglish (US)
Pages (from-to)88-91
Number of pages4
JournalNature
Volume374
Issue number6517
DOIs
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • General

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