Evidence map›Paper›PMID 21075849›Full record

ArticleThe Journal of biological chemistry2011

Roles of Dim2 in ribosome assembly.

Heather A Woolls, Allison C Lamanna, Katrin Karbstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. The FXR1 network acts as signaling scaffold for actomyosin remodeling.bioRxiv : the preprint server for biology · 2024
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  19. Structural Heterogeneity in Pre-40S Ribosomes.Structure (London, England : 1993) · 2017
    Article
  20. Article
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 at 1 institution in 1 country.

Heather A WoollsProgram in Chemical Biology, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
Allison C Lamanna
Katrin Karbstein
University of Michigan–Ann Arbor · US

Funding

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 R01 GM086451NIGMS NIH HHS R01-GM086451
6 · The paper itself

Abstract

In eukaryotes, ribosome assembly requires hundreds of conserved essential proteins not present in the mature particle. Despite their importance, the function of most factors remains unknown. This is because protein deletion often affects the composition of the entire particle. Additionally, many proteins are present in assembling ribosomes for extended times, which makes it difficult to pinpoint their role to a particular step. Here we have combined classical yeast biochemistry with experiments using recombinant proteins and RNA to study the role of Dim2 and its interaction with Nob1, the nuclease that generates the 3'-end of 18 S rRNA. Analysis of Dim2 mutants in which the interaction with Nob1 is disrupted demonstrates that this interaction between Dim2 and Nob1 is essential for optimal growth, and RNA binding experiments show that Dim2 increases Nob1 RNA affinity. Furthermore, our data indicate that Dim2 helps regulate Nob1 cleavage activity at the 3'-end of 18 S rRNA, as point mutants where this interaction is abolished in vitro accumulate pre-ribosomes containing Nob1 and 20 S rRNA in vivo. Interestingly, the site of interaction with Nob1 is mapped to the canonical RNA binding surface of a KH-like domain in Dim2, providing another example where an RNA-binding domain can be repurposed for protein interactions.

Indexed as

Binding SitesNuclear ProteinsPoint MutationRibosomesRNA, FungalRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDIM2 protein, S cerevisiaeNOB1 protein, S cerevisiaeNuclear ProteinsRNA, FungalRNA, Ribosomal, 18SSaccharomyces cerevisiae Proteins

Identifiers

PMID21075849
PMCPMC3024753
OpenAlexW2014079410

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.