Evidence map›Paper›PMID 11018011›Full record

ArticleGenes & development2000

Dynamic association of capping enzymes with transcribing RNA polymerase II.

S C Schroeder, B Schwer, S Shuman, D Bentley

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
–field-weighted citation impact
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

203 citing papers in PubMed, 384 citations in OpenAlex.

  1. The molecular basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2026
    Review
  2. CDK12 and CDK13 in oncology: from RNA regulation to therapeutic targeting.Cellular oncology (Dordrecht, Netherlands) · 2026
    Review
  3. Review
  4. Article
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  10. Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023
    Review
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  12. Review
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  14. Article
  15. Article
  16. Review
  17. Article
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  20. Article

143 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

4 authors at 2 institutions in 1 country.

S C SchroederDepartment of Biochemistry and Molecular Genetics, UCHSC, Denver, Colorado 80262, USA.
B Schwer
S Shuman
D Bentley
Kettering University · USCornell University · US

Funding

mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
Coupling of Transcription with Pre-mRNA MetabolismR01GM058613 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI BENTLEY, DAVID L · 1999 to 2014
$5.5M
NIGMS NIH HHS GM52470NIGMS NIH HHS GM58613NIGMS NIH HHS R01 GM052470NIGMS NIH HHS R01 GM058613
6 · The paper itself

Abstract

The C-terminal heptad repeat domain (CTD) of RNA polymerase II (pol II) is proposed to target pre-mRNA processing enzymes to nascent pol II transcripts, but this idea has not been directly tested in vivo. In vitro, the yeast mRNA capping enzymes Ceg1 and Abd1 bind specifically to the phosphorylated CTD. Here we show that yeast capping enzymes cross-link in vivo to the 5' ends of transcribed genes and that this localization requires the CTD. Both the extent of CTD phosphorylation at Ser 5 of the heptad repeat and the binding of capping enzymes decreased as polymerase moved from the 5' to the 3' ends of the ACT1, ENO2, TEF1, GAL1, and GAL10 genes. Ceg1 is released early in elongation, but Abd1 can travel with transcribing pol II as far as the 3' end of a gene. The CTD kinase, Kin28, is required for binding, and the CTD phosphatase, Fcp1, is required for dissociation of capping enzymes from the elongation complex. CTD phosphorylation and dephosphorylation therefore control the association of capping enzymes with pol II as it transcribes a gene.

Indexed as

Cyclin-Dependent KinasesRNA CapsSaccharomyces cerevisiae ProteinsTranscription, GeneticGenes, FungalMethyltransferasesmRNA GuanylyltransferasesNucleotidyltransferasesPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryRepetitive Sequences, Amino AcidRNA Polymerase IISaccharomyces cerevisiaeCyclin-Dependent KinasesKin28 protein kinase, S cerevisiaeMethyltransferasesmRNA (guanine(N7))-methyltransferasemRNA GuanylyltransferasesNucleotidyltransferasesPhosphoprotein PhosphatasesProtein Serine-Threonine KinasesRNA CapsRNA Polymerase IISaccharomyces cerevisiae Proteins

Identifiers

PMID11018011
PMCPMC316982
OpenAlexW2081322742

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.