Evidence map›Paper›PMID 26711263›Full record

ArticleMolecular and cellular biology2015

Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.

Jürgen Niesser, Felix R Wagner, Dirk Kostrewa, Wolfgang Mühlbacher, Patrick Cramer

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Structure of cytoplasmic RNA polymerase II.Nature communications · 2026
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  7. Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022
    Review
  8. Leg length and bristle density, both necessary for water surface locomotion, are genetically correlated in water striders.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
  11. Article
  12. Review
  13. Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source.Acta crystallographica. Section D, Structural biology · 2019
    Article
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Jürgen NiesserMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany Gene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Felix R WagnerGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Dirk KostrewaGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Wolfgang MühlbacherMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany.
Patrick CramerMax Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Göttingen, Germany pcramer@mpibpc.mpg.de.
Max Planck Institute for Biophysical Chemistry · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biogenesis of the 12-subunit RNA polymerase II (Pol II) transcription complex requires so-called GPN-loop GTPases, but the function of these enzymes is unknown. Here we report the first crystal structure of a eukaryotic GPN-loop GTPase, the Saccharomyces cerevisiae enzyme Npa3 (a homolog of human GPN1, also called RPAP4, XAB1, and MBDin), and analyze its catalytic mechanism. The enzyme was trapped in a GDP-bound closed conformation and in a novel GTP analog-bound open conformation displaying a conserved hydrophobic pocket distant from the active site. We show that Npa3 has chaperone activity and interacts with hydrophobic peptide regions of Pol II subunits that form interfaces in the assembled Pol II complex. Biochemical results are consistent with a model that the hydrophobic pocket binds peptides and that this can allosterically stimulate GTPase activity and subsequent peptide release. These results suggest that GPN-loop GTPases are assembly chaperones for Pol II and other protein complexes.

Indexed as

Amino Acid SequenceCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataMonomeric GTP-Binding ProteinsProtein ConformationProtein Structure, TertiaryProtein SubunitsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMonomeric GTP-Binding ProteinsNpa3 protein, S cerevisiaeProtein SubunitsRNA Polymerase IISaccharomyces cerevisiae Proteins

Identifiers

PMID26711263
PMCPMC4760217
OpenAlexW2205570383

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.