Evidence map›Paper›PMID 21709022›Full record

ArticleMolecular and cellular biology2011

H3K4 trimethylation by Set1 promotes efficient termination by the Nrd1-Nab3-Sen1 pathway.

Nihal Terzi, L Stirling Churchman, Lidia Vasiljeva, Jonathan Weissman, Stephen Buratowski

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
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  8. Review
  9. Review
  10. Article
  11. Structural and functional analysis of the SET3 histone deacetylase complex.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Interactions With Histone H3 & Tools to Study Them.Frontiers in cell and developmental biology · 2020
    Review
  18. Article
  19. Article
  20. 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 1 country.

Nihal TerziDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
L Stirling Churchman
Lidia Vasiljeva
Jonathan Weissman
Stephen Buratowski
Harvard University · USHoward Hughes Medical Institute · US

Funding

The RNA Polymerase II Transcription CycleR01GM056663 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Stephen Buratowski · 1999 to 2026
$11.7M
The RNA polymerase II transcription complexR01GM046498 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BURATOWSKI, STEPHEN · 1996 to 2024
$9.4M
RNA POLYMERASE II TRANSCRIPTION INITIATION COMPLEXR29GM046498 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI BURATOWSKI, STEPHEN · 1991 to 1995
–
NIGMS NIH HHS GM46498NIGMS NIH HHS GM56663NIGMS NIH HHS R01 GM046498NIGMS NIH HHS R01 GM056663
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the Nrd1-Nab3-Sen1 pathway mediates the termination of snoRNAs and cryptic unstable transcripts (CUTs). Both Nrd1 and the Set1 histone H3K4 methyltransferase complex interact with RNA polymerase II (Pol II) during early elongation, leading us to test whether these two processes are functionally linked. The deletion of SET1 exacerbates the growth rate and termination defects of nrd1 mutants. Set1 is important for the appropriate recruitment of Nrd1. Additionally, Set1 modulates histone acetylation levels in the promoter-proximal region via the Rpd3L deacetylase and NuA3 acetyltransferase complexes, both of which contain PHD finger proteins that bind methylated H3K4. Increased levels of histone acetylation reduce the efficiency of Nrd1-dependent termination. We speculate that Set1 promotes proper early termination by the Nrd1-Nab3-Sen1 complex by affecting the kinetics of Pol II transcription in early elongation.

Indexed as

AcetylationBlotting, NorthernChromatin ImmunoprecipitationDNA HelicasesHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesLysineMethylationMutationNuclear ProteinsPlasmidsProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsRNA HelicasesDNA HelicasesHistone DeacetylasesHistone-Lysine N-MethyltransferaseHistonesLysineNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsRNA HelicasesRNA Polymerase IIRNA, Small NucleolarRPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSEN1 protein, S cerevisiaeSET1 protein, S cerevisiae

Identifiers

PMID21709022
PMCPMC3165552
OpenAlexW2164372773

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.