Evidence map›Paper›PMID 27280440›Full record

ArticlePLoS biology2016

The DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation.

Sohail Khoshnevis, Isabel Askenasy, Matthew C Johnson, Maria D Dattolo, Crystal L Young-Erdos, M Elizabeth Stroupe, Katrin Karbstein

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

  1. Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  2. Effects ofExperimental and therapeutic medicine · 2026
    Article
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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.

Sohail KhoshnevisDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida, United States of America.
Isabel AskenasyDepartment of Biological Science and the Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, United States of America.
Matthew C JohnsonDepartment of Biological Science and the Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, United States of America.ORCID 0000-0002-1477-7801
Maria D DattoloDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida, United States of America.
Crystal L Young-ErdosDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida, United States of America.
M Elizabeth StroupeDepartment of Biological Science and the Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, United States of America.
Katrin KarbsteinDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida, United States of America.
Scripps Research Institute · USFlorida State University · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Quality Control in Ribosome Assembly - the Function of Regulatory ProteinsR01GM086451 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KARBSTEIN, KATRIN · 2009 to 2019
$4.8M
NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM086451
6 · The paper itself

Abstract

DEAD-box proteins are ubiquitous regulators of RNA biology. While commonly dubbed "helicases," their activities also include duplex annealing, adenosine triphosphate (ATP)-dependent RNA binding, and RNA-protein complex remodeling. Rok1, an essential DEAD-box protein, and its cofactor Rrp5 are required for ribosome assembly. Here, we use in vivo and in vitro biochemical analyses to demonstrate that ATP-bound Rok1, but not adenosine diphosphate (ADP)-bound Rok1, stabilizes Rrp5 binding to 40S ribosomes. Interconversion between these two forms by ATP hydrolysis is required for release of Rrp5 from pre-40S ribosomes in vivo, thereby allowing Rrp5 to carry out its role in 60S subunit assembly. Furthermore, our data also strongly suggest that the previously described accumulation of snR30 upon Rok1 inactivation arises because Rrp5 release is blocked and implicate a previously undescribed interaction between Rrp5 and the DEAD-box protein Has1 in mediating snR30 accumulation when Rrp5 release from pre-40S subunits is blocked.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateBinding SitesDEAD-box RNA HelicasesHydrolysisModels, MolecularMolecular ConformationNuclear ProteinsProtein BindingProtein DomainsRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsRNA, FungalRNA, Small NucleolarSaccharomyces cerevisiaeAdenosine DiphosphateAdenosine TriphosphateDEAD-box RNA HelicasesNuclear ProteinsRNA-Binding ProteinsRNA, FungalRNA, Small NucleolarROK1 protein, S cerevisiaeRRP5 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID27280440
PMCPMC4900678
OpenAlexW2412564419

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.