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PMID: 11478912 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Evidence that Gal11 protein is a target of the Gal4 activation domain in the mediator.

Biochemistry ·Vol. 40 ·No. 31 ·2001-08-07 ·Pages 9421-7

Jeong CJ, Yang SH, Xie Y, Zhang L, Johnston SA, Kodadek T

Abstract

The mediator is an approximately 20 protein complex that is essential for the transcription of most genes in yeast. It is contacted by a number of gene-specific activators, but the details of these interactions are not well understood in most cases. Here, evidence is presented that the mediator component Gal11 represents at least one target of the Gal4 activation domain (AD). Deletion of Gal11 is shown to decrease the affinity of the Gal4 AD for the mediator, and direct binding of an N-terminal domain of Gal11 with the Gal4 AD is demonstrated. Quantitative studies, however, indicate that the K(D) of the 1:1 Gal4 AD--Gal11 complex is modest. Combined with in vivo data showing that Delta gal11 cells exhibit reduced, but still significant, Gal4-mediated gene expression, these results suggest that the dimeric activator might also contact another protein in the mediator in addition to Gal11.

MeSH Terms
Binding, Competitive DNA-Binding Proteins Fungal Proteins/antagonists & inhibitors,genetics,metabolism,physiology Mediator Complex Peptide Fragments/genetics,metabolism Protein Binding/genetics Protein Structure, Tertiary/genetics Recombinant Fusion Proteins/metabolism Repressor Proteins/metabolism Saccharomyces cerevisiae Proteins Trans-Activators/genetics,metabolism,physiology Transcription Factors/antagonists & inhibitors,genetics,metabolism
Chemicals
DNA-Binding Proteins Fungal Proteins GAL11 protein, S cerevisiae GAL4 protein, S cerevisiae GAL80 protein, S cerevisiae Mediator Complex Peptide Fragments Recombinant Fusion Proteins Repressor Proteins Saccharomyces cerevisiae Proteins Trans-Activators Transcription Factors
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Jeong C J
Department of Internal Medicine, Ryburn Center for Molecular Cardiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8573, USA.
Yang S H
Xie Y
Zhang L
Johnston S A
Kodadek T
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
2001-08-07
Pages
9421-7
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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