Evidence map›Paper›PMID 11884590›Full record

ArticleMolecular and cellular biology2002

Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.

Melanie D Ohi, Andrew J Link, Liping Ren, Jennifer L Jennings, W Hayes McDonald, Kathleen L Gould

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

114 citing papers in PubMed, 221 citations in OpenAlex.

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  11. 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
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  12. Transcriptome ofInsects · 2022
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54 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Melanie D OhiHoward Hughes Medical Institute. Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
Andrew J Link
Liping Ren
Jennifer L Jennings
W Hayes McDonald
Kathleen L Gould
Howard Hughes Medical Institute · USVanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
MULTIDISCIPLINARY BASIC RESEARCH TRAINING IN CANCERT32CA009592 · NCI · VANDERBILT UNIVERSITY · PI Justin M Balko, Julie A Rhoades (Sterling) · 1987 to 2026
$10.4M
MECHANISMS OF EUKARYOTIC CELL CYCLE CONTROLR01GM047728 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 1992 to 2004
$989k
NCI NIH HHS 5P30CA68485NCI NIH HHS P30 CA068485NCI NIH HHS T32 CA009592NCI NIH HHS T32 CA09592NIGMS NIH HHS GM47728NIGMS NIH HHS R01 GM047728
6 · The paper itself

Abstract

Schizosaccharomyces pombe Cdc5p and its Saccharomyces cerevisiae ortholog, Cef1p, are essential Myb-related proteins implicated in pre-mRNA splicing and contained within large multiprotein complexes. Here we describe the tandem affinity purification (TAP) of Cdc5p- and Cef1p-associated complexes. Using transmission electron microscopy, we show that the purified Cdc5p complex is a discrete structure. The components of the S. pombe Cdc5p/S. cerevisiae Cef1p complexes (termed Cwfs or Cwcs, respectively) were identified using direct analysis of large protein complex (DALPC) mass spectrometry (A. J. Link et al., Nat. Biotechnol. 17:676-682, 1999). At least 26 proteins were detected in the Cdc5p/Cef1p complexes. Comparison of the polypeptides identified by S. pombe Cdc5p purification with those identified by S. cerevisiae Cef1p purification indicates that these two yeast complexes are nearly identical in composition. The majority of S. pombe Cwf proteins and S. cerevisiae Cwc proteins are known pre-mRNA splicing factors including core Sm and U2 and U5 snRNP components. In addition, the complex contains the U2, U5, and U6 snRNAs. Previously uncharacterized proteins were also identified, and we provide evidence that several of these novel factors are involved in pre-mRNA splicing. Our data represent the first comprehensive analysis of CDC5-associated proteins in yeasts, describe a discrete highly conserved complex containing novel pre-mRNA splicing factors, and demonstrate the power of DALPC for identification of components in multiprotein complexes.

Indexed as

ProteomeRNA SplicingAmino Acid SequenceAnimalsCell Cycle ProteinsHumansMacromolecular SubstancesMass SpectrometryMicroscopy, ElectronMolecular Sequence DataMolecular WeightMultiprotein ComplexesMutationProto-Oncogene Proteins c-mybRNA-Binding ProteinsRNA, Messengercdc5 protein, S pombeCEF1 protein, S cerevisiaeCell Cycle ProteinsMacromolecular SubstancesMultiprotein ComplexesProteomeProto-Oncogene Proteins c-mybRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA, Small NuclearSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID11884590
PMCPMC133674
OpenAlexW2117073299

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.