Evidence map›Paper›PMID 22407296›Full record

ArticleThe EMBO journal2012

Crystal structure of Cwc2 reveals a novel architecture of a multipartite RNA-binding protein.

Jana Schmitzová, Nicolas Rasche, Olexander Dybkov, Katharina Kramer, Patrizia Fabrizio, Henning Urlaub, Reinhard Lührmann, Vladimir Pena

Abstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Topology of the U12-U6ACS omega · 2020
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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.

Jana SchmitzováDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Nicolas Rasche
Olexander Dybkov
Katharina Kramer
Patrizia Fabrizio
Henning Urlaub
Reinhard Lührmann
Vladimir Pena

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast splicing factor Cwc2 contacts several catalytically important RNA elements in the active spliceosome, suggesting that Cwc2 is involved in determining their spatial arrangement at the spliceosome's catalytic centre. We have determined the crystal structure of the Cwc2 functional core, revealing how a previously uncharacterized Torus domain, an RNA recognition motif (RRM) and a zinc finger (ZnF) are tightly integrated in a compact folding unit. The ZnF plays a pivotal role in the architecture of the whole assembly. UV-induced crosslinking of Cwc2-U6 snRNA allowed the identification by mass spectrometry of six RNA-contacting sites: four in or close to the RRM domain, one in the ZnF and one on a protruding element connecting the Torus and RRM domains. The three distinct regions contacting RNA are connected by a contiguous and conserved positively charged surface, suggesting an expanded interface for RNA accommodation. Cwc2 mutations confirmed that the connector element plays a crucial role in splicing. We conclude that Cwc2 acts as a multipartite RNA-binding platform to bring RNA elements of the spliceosome's catalytic centre into an active conformation.

Indexed as

Base SequenceMolecular Sequence DataNucleotide MotifsProtein FoldingProtein Structure, TertiaryRNA-Binding ProteinsRNA PrecursorsRNA SplicingSaccharomyces cerevisiae ProteinsZinc FingersCwc2 protein, S cerevisiaeRNA-Binding ProteinsRNA PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID22407296
PMCPMC3343462

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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.