Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex.

The Journal of biological chemistry - 13 Oct 2000

Xie Y, Denison C, Yang S H, Fancy D A, Kodadek T

Abstract excerpt

It has been suggested that complexes between gene-specific activators and the TATA-binding protein (TBP) play an important role in the expression of many genes. However, few detailed studies of well defined activator-TBP complexes have been reported. An analysis of the biochemical properties of the complex formed by the acidic activation domain (AAD) of the yeast activator Gal4 and TBP is presented here. This is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Cross-Linking Reagents
Share to Fluorescence Polarization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Macromolecular Substances

Share to Peptide Fragments

Share to TATA Box

Share to TATA-Box Binding Protein

Share to Yeasts

Source

Identifiers

PMID: 10931832
DOI: 10.1074/jbc.M003760200

Genes

TBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical characterization of the TATA-binding protein-Gal4 activation domain complex.PMID 10931832Read ↗

The Drosophila TATA binding protein contains a strong but masked activation domain.Semantic proximity Read ↗

Connecting a promoter-bound protein to TBP bypasses the need for a transcriptional activation domain.Semantic proximity Read ↗

Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro.Semantic proximity Read ↗

Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo.Semantic proximity Read ↗

Analysis of structure-function relationships of yeast TATA box binding factor TFIID.Semantic proximity Read ↗

Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo.Semantic proximity Read ↗

Mutations on the DNA-binding surface of TATA-binding protein can specifically impair the response to acidic activators in vivo.Semantic proximity Read ↗

Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor.Semantic proximity Read ↗

Does the human immunodeficiency virus Tat trans-activator contain a discrete activation domain?Semantic proximity Read ↗

A Random Screen Using a Novel Reporter Assay System Reveals a Set of Sequences That Are Preferred as the TATA or TATA-Like Elements in the CYC1 Promoter of Saccharomyces cerevisiae.Semantic proximity Read ↗

TFIIA interacts with TFIID via association with TATA-binding protein and TAF40.Semantic proximity Read ↗

Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.