Evidence map›Paper›PMID 23328630›Full record

ReviewRNA biology2013

xRRM: a new class of RRM found in the telomerase La family protein p65.

Mahavir Singh, Charles P Choi, Juli Feigon

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. A (Scientific) Lifetime Affair With Nucleic Acids.Journal of molecular biology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structure ofRNA biology · 2021
    Article
  8. Review
  9. Review
  10. Review
  11. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Article
  13. RRMdb-an evolutionary-oriented database of RNA recognition motif sequences.Database : the journal of biological databases and curation · 2019
    Article
  14. Article
  15. Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Article
  18. Review
  19. Reconstitution of a functional 7SK snRNP.Nucleic acids research · 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.

Mahavir SinghDepartment of Chemistry and Biochemistry and the Molecular Biology Institute; University of California; Los Angeles, CA USA.
Charles P Choi
Juli Feigon
University of California System · US

Funding

STRUCTURE OF TELOMERIC DNA OLIGONUCLEOTIDESR01GM048123 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1992 to 2018
$6.4M
NIGMS NIH HHS GM48123NIGMS NIH HHS R01 GM048123
6 · The paper itself

Abstract

Genuine La and La-related proteins group 7 (LARP7) bind to the non-coding RNAs transcribed by RNA polymerase III (RNAPIII), which end in UUU-3'OH. The La motif and RRM1 of these proteins (the La module) cooperate to bind the UUU-3'OH, protecting the RNA from degradation, while other domains may be important for RNA folding or other functions. Among the RNAPIII transcripts is ciliate telomerase RNA (TER). p65, a member of the LARP7 family, is an integral Tetrahymena thermophila telomerase holoenzyme protein required for TER biogenesis and telomerase RNP assembly. p65, together with TER and telomerase reverse transcriptase (TERT), form the Tetrahymena telomerase RNP catalytic core. p65 has an N-terminal domain followed by a La module and a C-terminal domain, which binds to the TER stem 4. We recently showed that the p65 C-terminal domain harbors a cryptic, atypical RRM, which uses a unique mode of single- and double-strand RNA binding and is required for telomerase RNP catalytic core assembly. This domain, which we named xRRM, appears to be present in and unique to genuine La and LARP7 proteins. Here we review the structure of the xRRM, discuss how this domain could recognize diverse substrates of La and LARP7 proteins and discuss the functional implications of the xRRM as an RNP chaperone.

Indexed as

Amino Acid MotifsCatalytic DomainModels, MolecularNuclear ProteinsNucleic Acid ConformationPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryProtozoan ProteinsRNARNA FoldingRNA, ProtozoanTelomeraseTetrahymena thermophilaNuclear ProteinsPdd1 protein, TetrahymenaPhosphoproteinsProtozoan ProteinsRNARNA, ProtozoanTelomerasetelomerase RNALa proteinLARP7p65RNA conformationtelomerasetelomerase RNATetrahymenaxRRM2

Identifiers

PMID23328630
PMCPMC3672277
OpenAlexW2072982592

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.