The Yeast TAF145 Inhibitory Domain and TFIIA Competitively Bind to TATA-binding Protein

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1998 Feb 3

PMID 9447997

Citations 64

Authors

T Kokubo

M J SWANSON

J I Nishikawa

A G Hinnebusch

Y Nakatani

Affiliations

Soon will be listed here.

Abstract

The Drosophila 230-kDa TFIID subunit (dTAF230) interacts with the DNA binding domain of TATA box-binding protein (TBP) which exists in the same complex. Here, we characterize the inhibitory domain in the yeast TAF145 (yTAF145), which is homologous to dTAF230. Mutation studies show that the N-terminal inhibitory region (residues 10 to 71) can be divided into two subdomains, I (residues 10 to 37) and II (residues 46 to 71). Mutations in either subdomain significantly impair function. Acidic residues in subdomain II are important for the interaction with TBP. In addition, yTAF145 interaction is impaired by mutating the basic residues on the convex surface of TBP, which are crucial for interaction with TFIIA. Consistently, TFIIA and yTAF145 bind competitively to TBP. A deletion of the inhibitory domain of yTAF145 leads to a temperature-sensitive growth phenotype. Importantly, this phenotype is suppressed by overexpression of the TFIIA subunits, indicating that the yTAF145 inhibitory domain is involved in TFIIA function.

Citing Articles

TFIID dependency of steady-state mRNA transcription altered epigenetically by simultaneous functional loss of Taf1 and Spt3 is Hsp104-dependent.

Iwami R, Takai N, Matsutani M, Shiwa Y, Kokubo H, Kasahara K PLoS One. 2023; 18(2):e0281233.

PMID: 36757926 PMC: 9910645. DOI: 10.1371/journal.pone.0281233.

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Structure of human TFIID and mechanism of TBP loading onto promoter DNA.

Patel A, Louder R, Greber B, Grunberg S, Luo J, Fang J Science. 2018; 362(6421).

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SAGA mediates transcription from the TATA-like element independently of Taf1p/TFIID but dependent on core promoter structures in Saccharomyces cerevisiae.

Watanabe K, Kokubo T PLoS One. 2017; 12(11):e0188435.

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Towards a mechanistic understanding of core promoter recognition from cryo-EM studies of human TFIID.

Nogales E, Patel A, Louder R Curr Opin Struct Biol. 2017; 47:60-66.

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