Evidence map›Paper›PMID 27340124›Full record

ArticleThe EMBO journal2016

Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.

Karen S Conrad, Jennifer M Hurley, Joanne Widom, Carol S Ringelberg, Jennifer J Loros, Jay C Dunlap, Brian R Crane

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
8.2field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  13. GIpred: a computational tool for prediction of GIGANTEA proteins using machine learning algorithm.Physiology and molecular biology of plants : an international journal of functional plant biology · 2022
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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

7 authors at 2 institutions in 1 country.

Karen S ConradDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.
Jennifer M HurleyDepartment of Genetics, Geisel School of Medicine, Hanover, NH, USA.
Joanne WidomDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA.
Carol S RingelbergDepartment of Genetics, Geisel School of Medicine, Hanover, NH, USA.
Jennifer J LorosDepartment of Biochemistry, Geisel School of Medicine, Hanover, NH, USA.
Jay C DunlapDepartment of Genetics, Geisel School of Medicine, Hanover, NH, USA.
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, USA bc69@cornell.edu.ORCID 0000-0001-8234-9991
Dartmouth College · USCornell University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Genetic and Molecular Dissection of the Neurospora ClockR35GM118021 · NIGMS · DARTMOUTH COLLEGE · PI Jay C. Dunlap · 2016 to 2026
$7.3M
GENETIC AND MOLECULAR DISSECTION OF THE NEUROSPORA CLOCKR01GM034985 · NIGMS · DARTMOUTH COLLEGE · PI DUNLAP, JAY C. · 1986 to 2015
$5.7M
GENETIC AND MOLECULAR DISSECTION OF THE NEUSPORA CLOCKR37GM034985 · NIGMS · DARTMOUTH COLLEGE · PI DUNLAP, JAY C · 1998 to 2007
$4.4M
Identification and Analysis of Circadian Clock-Controlled GenesR35GM118022 · NIGMS · DARTMOUTH COLLEGE · PI LOROS, JENNIFER J. · 2016 to 2021
$3.7M
Structure and Function of Circadian Clock Light SensorsR01GM079679 · NIGMS · CORNELL UNIVERSITY · PI CRANE, BRIAN R · 2007 to 2016
$3.1M
Structural and Computational Studies of LOV domain proteins and CryptochromesF32GM099391 · NIGMS · CORNELL UNIVERSITY · PI CONRAD, KAREN S · 2012 to 2013
$101k
NIGMS NIH HHS F32 GM099391NIGMS NIH HHS P41 GM103403NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM034985NIGMS NIH HHS R01 GM079679NIGMS NIH HHS R35 GM118021NIGMS NIH HHS R35 GM118022NIGMS NIH HHS R37 GM034985
6 · The paper itself

Abstract

In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA Helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH crystal structures in several conformations and bound to ADP/RNA reveal differences between FRH and the yeast homolog Mtr4 that clarify the distinct role of FRH in the clock. The FRQ-interacting region at the FRH N-terminus has variable structure in the absence of FRQ A known mutation that disrupts circadian rhythms (R806H) resides in a positively charged surface of the KOW domain, far removed from the helicase core. We show that changes to other similarly located residues modulate interactions with the WCC and FRQ A V142G substitution near the N-terminus also alters FRQ and WCC binding to FRH, but produces an unusual short clock period. These data support the assertion that FRH helicase activity does not play an essential role in the clock, but rather FRH acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module.

Indexed as

Circadian ClocksCrystallography, X-RayFungal ProteinsModels, MolecularMutant ProteinsNeurospora crassaProtein BindingProtein ConformationProtein DomainsRNA HelicasesFRH protein, Neurospora crassaFungal ProteinsMutant ProteinsRNA Helicaseschaperonecircadian clockprotein interactionsprotein structuretranscriptional repressor

Identifiers

PMID27340124
PMCPMC4969578
OpenAlexW2463149511

What OpenQuestion holds

Textmetadata
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.