Evidence map›Paper›PMID 10852970›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

The C-terminal domain-phosphorylated IIO form of RNA polymerase II is associated with the transcription repressor NC2 (Dr1/DRAP1) and is required for transcription activation in human nuclear extracts.

E Castaño, P Gross, Z Wang, R G Roeder, T Oelgeschläger

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-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

14 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Regulation of nuclear import and export of negative cofactor 2.The Journal of biological chemistry · 2009
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Direct stimulation of transcription by negative cofactor 2 (NC2) through TATA-binding protein (TBP).Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  13. Article
  14. 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

5 authors at 2 institutions in 2 countries.

E CastañoEukaryotic Gene Regulation Laboratory, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, United Kingdom.
P Gross
Z Wang
R G Roeder
T Oelgeschläger
Rockefeller University · USMarie Curie · GB

Funding

BIOCHEMICAL MECHANISMS OF HIV TRANSCRIPTIONAL REGULATIONR01AI037327 · NIAID · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 1995 to 1999
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MOLECULAR BASIS OF CELL GROWTH AND TRANSFORMATIONR35CA042567 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 1986 to 1999
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NCI NIH HHS CA42567NIAID NIH HHS AI37327
6 · The paper itself

Abstract

Activation of class II gene transcription may involve alleviation of transcription repression as well as stimulation of the assembly and function of the general RNA polymerase (RNAP) II transcription machinery. Here, we investigated whether activator-reversible transcription repression by NC2 (Dr1/DRAP1) contributes to maximum induction levels in unfractionated HeLa nuclear extracts. Surprisingly, we found that depletion of NC2 does not significantly affect basal transcription, but dramatically reduces activated transcription. Immunoblot analyses revealed that the loss of activator function coincides with selective removal of the C-terminal domain (CTD)-hyperphosphorylated RNAP IIO along with NC2. Coimmunoprecipitation experiments with purified factors confirmed that NC2 interacts with RNAP IIO, but not with the unphosphorylated or hypophosphorylated RNAP IIA or CTD-less RNAP IIB forms. Finally, we demonstrate that, in contrast to previously published observations in cell-free systems reconstituted with purified factors, only the CTD-phosphorylated form of RNAP II can mediate activator function in the context of unfractionated HeLa nuclear extracts. These findings reveal an unexpected link between NC2 and transcription activation and suggest that regulation of RNAP II transcription through reversible CTD phosphorylation might be more complex than previously proposed.

Indexed as

Transcriptional ActivationAnimalsCell NucleusHistocompatibility Antigens Class IIHumansPhosphoproteinsPhosphorylationRatsRNA Polymerase IITATA BoxTranscription Factorsdown-regulator of transcription 1Histocompatibility Antigens Class IIPhosphoproteinsRNA Polymerase IITranscription Factors

Identifiers

PMID10852970
PMCPMC16520
OpenAlexW1967334341

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.