Evidence map›Paper›PMID 31751889›Full record

ReviewCurrent opinion in structural biology2020

Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.

Avinash B Patel, Basil J Greber, Eva Nogales

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Avinash B PatelMolecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Electronic address: patelab@berkeley.edu.
Basil J GreberMolecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA.
Eva NogalesMolecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA; Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA. Electronic address: ENogales@lbl.gov.

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Structural studies of function and regulation of microtubules and transcriptional gene expression machineryR35GM127018 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Eva Nogales · 2018 to 2026
$4.3M
Structural Studies of the Eukaryotic Transcription Initiation MachineryR01GM063072 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI NOGALES, EVA · 2001 to 2016
$2.5M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM063072NIGMS NIH HHS R35 GM127018NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

TFIID is a large multiprotein assembly that serves as a general transcription factor for transcription initiation by eukaryotic RNA polymerase II (Pol II). TFIID is involved in the recognition of the core promoter sequences and neighboring chromatin marks, and can interact with gene-specific activators and repressors. In order to obtain a better molecular and mechanistic understanding of the function of TFIID, its structure has been pursued for many years. However, the scarcity of TFIID and its highly flexible nature have made this pursuit very challenging. Recent breakthroughs, largely due to methodological advances in cryo-electron microscopy, have finally described the structure of this complex, both alone and engaged with core promoter DNA, revealing the functional significance of its conformational complexity in the process of core promoter recognition and initiation of Pol II transcription. Here, we review these recent structural insights and discuss their implications for our understanding of eukaryotic transcription initiation.

Indexed as

Molecular Docking SimulationMolecular Dynamics SimulationPromoter Regions, GeneticProtein ConformationAmino Acid SequenceFungal ProteinsHumansMolecular ConformationProtein BindingStructure-Activity RelationshipTATA-Box Binding ProteinTranscription Factor TFIIDFungal ProteinsTATA-Box Binding ProteinTranscription Factor TFIID

Identifiers

PMID31751889
PMCPMC7156316

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.