Cited by 450Genomics and Chromatin DynamicsFungal and yeast genetics researchNuclear Structure and Function

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A novel mediator between activator proteins and the RNA polymerase II transcription apparatus

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Kelleher, Raymond J., Flanagan, Peter M., Kornberg, Roger D.·1990·Cell

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Abstract

One gene activator protein may interfere with the effects of another in eukaryotic cells. We report here that a hybrid yeast-herpes gene activator protein inhibits transcriptional activation by a thymidine-rich DNA element in yeast. This example of activator interference can be faithfully reproduced in vitro. Interference is reversed by a partially purified yeast component, but not by RNA polymerase II or various polymerase II transcription factors. We conclude that the partially purified yeast component is a novel factor, and we suggest this factor mediates the transcriptional activation process.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
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Transformation of intact yeast cells treated with alkali cations.
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Method
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BackgroundInfluentialSelf-citation

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Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
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Background
Identification of Human Proteins Functionally Conserved with the Yeast Putative Adaptors ADA2 and GCN5
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BackgroundMethodInfluential
Characterization of Physical Interactions of the Putative Transcriptional Adaptor, ADA2, with Acidic Activation Domains and TATA-binding Protein
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An Activator Binding Module of Yeast RNA Polymerase II Holoenzyme
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Hyperphosphorylation of the C-terminal Repeat Domain of RNA Polymerase II Facilitates Dissociation of Its Complex with Mediator*
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Background

Authors: Kelleher, R. J., Flanagan, P. M., & Kornberg, R. D.
Affiliations: Stanford Medicine (US)
ORCID: Kornberg, Roger D.
Venue: Cell
Publisher: Elsevier BV
Published: 1990-06
Volume: 61
Issue: 7
Pages: 1209-1215
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(90)90685-8
OpenAlex: W2021893003
Cited by: 450
References: 35
Citations by year: 2026: 5 · 2025: 6 · 2024: 10 · 2023: 3 · 2022: 5 · 2021: 13 · 2020: 20 · 2019: 12 · 2018: 14 · 2017: 10 · 2016: 8 · 2015: 8 · 2014: 10 · 2013: 16 · 2012: 8
FWCI: 20.26
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 5436 d)
Locations: Cell (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Funders: National Institutes of Health (GM-07365, GM-36859)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: RNA polymerase II, transcriptional activation, transcriptional coactivator, transcription factors
MeSH terms: beta-Galactosidase, Cell Nucleus, DNA-Binding Proteins, DNA, Fungal, Fungal Proteins, Kinetics, Phosphoproteins, Plasmids, Recombinant Fusion Proteins, RNA Polymerase II, Saccharomyces cerevisiae, Transcription Factors, Transcription, Genetic, Trans-Activators, Gene Expression Regulation, Fungal, Simplexvirus, Saccharomyces cerevisiae Proteins

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A novel mediator between activator proteins and the RNA polymerase II transcription apparatus

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