Evidence map›Paper›PMID 15632056›Full record

ArticleMolecular and cellular biology2005

The C-terminal domain of RNA polymerase II functions as a phosphorylation-dependent splicing activator in a heterologous protein.

Scott Millhouse, James L Manley

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
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  6. Sleep loss disrupts Arc expression in dentate gyrus neurons.Neurobiology of learning and memory · 2019
    Article
  7. The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019
    Review
  8. Review
  9. Article
  10. Co-transcriptional mRNP formation is coordinated within a molecular mRNP packaging station in S. cerevisiae.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. TLS inhibits RNA polymerase III transcription.Molecular and cellular biology · 2010
    Article
  20. Neuronal cell depolarization induces intragenic chromatin modifications affecting NCAM alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

2 authors at 1 institution in 1 country.

Scott MillhouseDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
James L Manley
Columbia University · US

Funding

MECHANISMS OF ALTERNATIVE SPLICING OF PRE MRNAR37GM048259 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1996 to 2005
$2.8M
RNA Pol II CTD enhances early spliceosome assemblyF32GM063322 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MILLHOUSE, SCOTT R · 2001 to 2003
$127k
NIGMS NIH HHS F32 GM063322NIGMS NIH HHS R37 GM048259NIGMS NIH HHS R37 GM48259
6 · The paper itself

Abstract

RNA polymerase II, and specifically the C-terminal domain (CTD) of its largest subunit, has been demonstrated to play important roles in capping, splicing, and 3' processing of mRNA precursors. But how the CTD functions in these reactions, especially splicing, is not well understood. To address some of the basic questions concerning CTD function in splicing, we constructed and purified two fusion proteins, a protein in which the CTD is positioned at the C terminus of the splicing factor ASF/SF2 (ASF-CTD) and an RS domain deletion mutant protein (ASFDeltaRS-CTD). Significantly, compared to ASF/SF2, ASF-CTD increased the reaction rate during the early stages of splicing, detected as a 20- to 60-min decrease in splicing lag time depending on the pre-mRNA substrate. The increased splicing rate correlated with enhanced production of prespliceosomal complex A and the early spliceosomal complex B but, interestingly, not the very early ATP-independent complex E. Additional assays indicate that the RS domain and CTD perform distinct functions, as exemplified by our identification of an activity that cooperates only with the CTD. Dephosphorylated ASFDeltaRS-CTD and a glutathione S-transferase-CTD fusion protein were both inactive, suggesting that an RNA-targeting domain and CTD phosphorylation were necessary. Our results provide new insights into the mechanism by which the CTD functions in splicing.

Indexed as

RNA SplicingAmino Acid SequenceAnimalsNuclear ProteinsPhosphorylationProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase IIRNA PrecursorsSerineSpliceosomesSubcellular FractionsNuclear ProteinsProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase IIRNA PrecursorsSerine

Identifiers

PMID15632056
PMCPMC543425
OpenAlexW1974453049

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.