Evidence map›Paper›PMID 20826804›Full record

ArticleThe Journal of biological chemistry2010

The archaeal Lsm protein binds to small RNAs.

Susan Fischer, Juliane Benz, Bettina Späth, Lisa-Katharina Maier, Julia Straub, Michaela Granzow, Monika Raabe, Henning Urlaub, Jan Hoffmann, Bernd Brutschy and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
2.3field-weighted citation impact, top 12% 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, 79 citations in OpenAlex.

  1. Article
  2. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  3. Article
  4. Analysis of Lsm Protein-Mediated Regulation in the HaloarchaeonInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Genes · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. The sole LSm complex inRNA (New York, N.Y.) · 2017
    Article
  19. 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

13 authors at 4 institutions in 2 countries.

Susan FischerBiology II, Ulm University, 89069 Ulm, Germany.
Juliane Benz
Bettina Späth
Lisa-Katharina Maier
Julia Straub
Michaela Granzow
Monika Raabe
Henning Urlaub
Jan Hoffmann
Bernd Brutschy
Thorsten Allers
Jörg Soppa
Anita Marchfelder
Goethe University Frankfurt · DEUniversität Ulm · DEMax Planck Institute for Biophysical Chemistry · DEUniversity of Nottingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of the Lsm family, including eukaryotic Sm proteins and bacterial Hfq, are key players in RNA metabolism. Little is known about the archaeal homologues of these proteins. Therefore, we characterized the Lsm protein from the haloarchaeon Haloferax volcanii using in vitro and in vivo approaches. H. volcanii encodes a single Lsm protein, which belongs to the Lsm1 subfamily. The lsm gene is co-transcribed and overlaps with the gene for the ribosomal protein L37e. Northern blot analysis shows that the lsm gene is differentially transcribed. The Lsm protein forms homoheptameric complexes and has a copy number of 4000 molecules/cell. In vitro analyses using electrophoretic mobility shift assays and ultrasoft mass spectrometry (laser-induced liquid bead ion desorption) showed a complex formation of the recombinant Lsm protein with oligo(U)-RNA, tRNAs, and an small RNA. Co-immunoprecipitation with a FLAG-tagged Lsm protein produced in vivo confirmed that the protein binds to small RNAs. Furthermore, the co-immunoprecipitation revealed several protein interaction partners, suggesting its involvement in different cellular pathways. The deletion of the lsm gene is viable, resulting in a pleiotropic phenotype, indicating that the haloarchaeal Lsm is involved in many cellular processes, which is in congruence with the number of protein interaction partners.

Indexed as

Archaeal ProteinsHaloferax volcaniiMass SpectrometryPoly UProtein BindingProtein MultimerizationRibosomal ProteinsRNA, ArchaealRNA-Binding ProteinsRNA, TransferTranscription, GeneticArchaeal ProteinsPoly URibosomal ProteinsRNA, ArchaealRNA-Binding ProteinsRNA, Transfer

Identifiers

PMID20826804
PMCPMC2966057
OpenAlexW2034064568

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.