Evidence map›Paper›PMID 28945358›Full record

ArticleBiochemistry2018

Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment.

Abigail M Janke, Da Hee Seo, Vahid Rahmanian, Alexander E Conicella, Kaylee L Mathews, Kathleen A Burke, Jeetain Mittal, Nicolas L Fawzi

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  4. Phase separation of the oncogenic fusion protein EWS::FLI1 is modulated by its DNA-binding domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Phase-Separated Subcellular Compartmentation and Related Human Diseases.International journal of molecular sciences · 2022
    Review
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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

8 authors at 2 institutions in 1 country.

Abigail M JankeDepartment of Molecular Pharmacology, Physiology, and Biotechnology , Brown University , Providence , Rhode Island 02921 , United States.
Da Hee SeoDepartment of Molecular Pharmacology, Physiology, and Biotechnology , Brown University , Providence , Rhode Island 02921 , United States.
Vahid RahmanianDepartment of Chemical and Biomolecular Engineering , Lehigh University , Bethlehem , Pennsylvania 18015 , United States.
Alexander E ConicellaGraduate Program in Molecular Biology, Cell Biology and Biochemistry , Brown University , Providence , Rhode Island 02912 , United States.
Kaylee L MathewsGraduate Program in Molecular Biology, Cell Biology and Biochemistry , Brown University , Providence , Rhode Island 02912 , United States.
Kathleen A BurkeDepartment of Molecular Pharmacology, Physiology, and Biotechnology , Brown University , Providence , Rhode Island 02921 , United States.
Jeetain MittalDepartment of Chemical and Biomolecular Engineering , Lehigh University , Bethlehem , Pennsylvania 18015 , United States.
Nicolas L FawziDepartment of Molecular Pharmacology, Physiology, and Biotechnology , Brown University , Providence , Rhode Island 02921 , United States.ORCID 0000-0001-5483-0577
Brown University · USLehigh University · US

Funding

UTERINE NK CELL HOMING FROM THE PERIPHERAL CIRCULATIONP20RR018728 · NCRR · WOMEN AND INFANTS HOSPITAL-RHODE ISLAND · PI BLISS, JOSEPH MARK · 2003 to 2011
$16.7M
COBRE for Skeletal Health and RepairP20GM104937 · NIGMS · RHODE ISLAND HOSPITAL · PI CHEN, QIAN · 2012 to 2016
$10.8M
Pilot Projects ProgramP30GM122732 · NIGMS · RHODE ISLAND HOSPITAL · PI CHEN, QIAN · 2017 to 2021
$6.6M
TRAINING IN MOLECULAR &CELL BIOLOGY &BIOCHEMISTRYT32GM007601 · NIGMS · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L. · 1985 to 2019
$6.4M
Center for Cancer Signaling NetworksP30GM103410 · NIGMS · BROWN UNIVERSITY · PI ATWOOD, WALTER J · 2012 to 2015
$4.3M
Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
CENTER FOR CANCER SIGNALING NETWORKSP30RR031153 · NCRR · BROWN UNIVERSITY · PI ATWOOD, WALTER J · 2011 to 2011
$1.1M
Acquisition of an Orbitrap XL ETD Mass Spectrometer through Upgrading an LTQS10RR027027 · NCRR · BROWN UNIVERSITY · PI HAWROT, EDWARD · 2010 to 2010
$500k
CD SPECTROPHOTOMETER: STRUCTURAL BIOL, PROTEIN, MOLECULAR PHARMACOLOGYS10RR020923 · NCRR · BROWN UNIVERSITY · PI MIERKE, DALE F · 2006 to 2006
$105k
NCRR NIH HHS P20 RR018728NCRR NIH HHS P30 RR031153NCRR NIH HHS S10 RR020923NCRR NIH HHS S10 RR027027NIGMS NIH HHS P20 GM104937NIGMS NIH HHS P30 GM103410NIGMS NIH HHS P30 GM122732NIGMS NIH HHS R01 GM118530NIGMS NIH HHS T32 GM007601
6 · The paper itself

Abstract

Many cancer-causing chromosomal translocations result in transactivating protein products encoding FET family (FUS, EWSR1, TAF15) low-complexity (LC) domains fused to a DNA binding domain from one of several transcription factors. Recent work demonstrates that higher-order assemblies of FET LC domains bind the carboxy-terminal domain of the large subunit of RNA polymerase II (RNA pol II CTD), suggesting FET oncoproteins may mediate aberrant transcriptional activation by recruiting RNA polymerase II to promoters of target genes. Here we use nuclear magnetic resonance (NMR) spectroscopy and hydrogel fluorescence microscopy localization and fluorescence recovery after photobleaching to visualize atomic details of a model of this process, interactions of RNA pol II CTD with high-molecular weight TAF15 LC assemblies. We report NMR resonance assignments of the intact degenerate repeat half of human RNA pol II CTD alone and verify its predominant intrinsic disorder by molecular simulation. By measuring NMR spin relaxation and dark-state exchange saturation transfer, we characterize the interaction of RNA pol II CTD with amyloid-like hydrogel fibrils of TAF15 and hnRNP A2 LC domains and observe that heptads far from the acidic C-terminal tail of RNA pol II CTD bind TAF15 fibrils most avidly. Mutation of CTD lysines in heptad position 7 to consensus serines reduced the overall level of TAF15 fibril binding, suggesting that electrostatic interactions contribute to complex formation. Conversely, mutations of position 7 asparagine residues and truncation of the acidic tail had little effect. Thus, weak, multivalent interactions between TAF15 fibrils and heptads throughout RNA pol II CTD collectively mediate complex formation.

Indexed as

Transcription, GeneticHeterogeneous-Nuclear Ribonucleoprotein Group A-BHumansLysineMagnetic Resonance SpectroscopyMultiprotein ComplexesMutationNeoplasmsPromoter Regions, GeneticProtein BindingProtein DomainsRNA Polymerase IITATA-Binding Protein Associated FactorsTranslocation, GeneticHeterogeneous-Nuclear Ribonucleoprotein Group A-BhnRNP A2LysineMultiprotein ComplexesRNA Polymerase IITAF15 protein, humanTATA-Binding Protein Associated Factors

Identifiers

PMID28945358
PMCPMC5975632
OpenAlexW2758648654

What OpenQuestion holds

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Registered trials

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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.