Evidence map›Paper›PMID 15075370›Full record

ArticleMolecular biology of the cell2004

An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5.

Cesar F Fernandez, Barbara K Pannone, Xinguo Chen, Gabriele Fuchs, Sandra L Wolin

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of transient intermediates during spliceosome activation by single molecule fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Core spliceosomal Sm proteins as constituents of cytoplasmic mRNPs in plants.The Plant journal : for cell and molecular biology · 2020
    Article
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  8. Review
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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 1 institution in 1 country.

Cesar F FernandezDepartment of Cell Biology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06536, USA.
Barbara K Pannone
Xinguo Chen
Gabriele Fuchs
Sandra L Wolin
Howard Hughes Medical Institute · US

Funding

Biogenesis of Small RNAsR01GM048410 · NIGMS · YALE UNIVERSITY · PI WOLIN, SANDRA L. · 1998 to 2009
$2.2M
NIGMS NIH HHS R01 GM048410NIGMS NIH HHS R01-GM48410
6 · The paper itself

Abstract

Sm-like (Lsm) proteins function in a variety of RNA-processing events. In yeast, the Lsm2-Lsm8 complex binds and stabilizes the spliceosomal U6 snRNA, whereas the Lsm1-Lsm7 complex functions in mRNA decay. Here we report that a third Lsm complex, consisting of Lsm2-Lsm7 proteins, associates with snR5, a box H/ACA snoRNA that functions to guide site-specific pseudouridylation of rRNA. Experiments in which the binding of Lsm proteins to snR5 was reconstituted in vitro reveal that the 3' end of snR5 is critical for Lsm protein recognition. Glycerol gradient sedimentation and sequential immunoprecipitation experiments suggest that the Lsm protein-snR5 complex is partly distinct from the complex formed by snR5 RNA with the box H/ACA proteins Gar1p and Nhp2p. Consistent with a separate complex, Lsm proteins are not required for the function of snR5 in pseudouridylation of rRNA. We demonstrate that in addition to their known nuclear and cytoplasmic locations, Lsm proteins are present in nucleoli. Taken together with previous findings that a small fraction of pre-RNase P RNA associates with Lsm2-Lsm7, our experiments suggest that an Lsm2-Lsm7 protein complex resides in nucleoli, contributing to the biogenesis or function of specific snoRNAs.

Indexed as

Base SequenceCell NucleolusMolecular Sequence DataMultiprotein ComplexesProtein BindingRibonucleoproteins, Small NuclearRNA, FungalRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityLsm2 protein, S cerevisiaeMultiprotein ComplexesRibonucleoproteins, Small NuclearRNA, FungalRNA, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID15075370
PMCPMC420107
OpenAlexW2106543077

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.