Evidence map›Paper›PMID 23401858›Full record

ArticleMolecular and cellular biology2013

Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation.

Yu-Ming Xue, Anna K Kowalska, Kamila Grabowska, Katarzyna Przybyt, Magda A Cichewicz, Brian C Del Rosario, Lucy F Pemberton

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. 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
1.6field-weighted citation impact, top 16% 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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
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

7 authors at 1 institution in 1 country.

Yu-Ming XueDepartment of Microbiology, Immunology and Cancer Biology, Center for Cell Signaling, University of Virginia, Charlottesville, Virginia, USA.
Anna K Kowalska
Kamila Grabowska
Katarzyna Przybyt
Magda A Cichewicz
Brian C Del Rosario
Lucy F Pemberton
University of Virginia · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
Cancer Research Training Program: From Molecular Mechanisms to Therapeutic StrategiesT32CA009109 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Andrew Carl Dudley, Melanie R Rutkowski · 1985 to 2026
$13.9M
HISTONE NUCLEAR IMPORT AND CHROMATIN ASSEMBLYR01GM065385 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PEMBERTON, LUCY F · 2002 to 2010
$2.7M
NCI NIH HHS P30 CA044579NCI NIH HHS T32 CA009109NIGMS NIH HHS R01 GM065385NIGMS NIH HHS R01 GM65385
6 · The paper itself

Abstract

Histone chaperones function in chromatin assembly and disassembly, suggesting they have important regulatory roles in transcription elongation. The Saccharomyces cerevisiae proteins Nap1 and Vps75 are structurally related, evolutionarily conserved histone chaperones. We showed that Nap1 genetically interacts with several transcription elongation factors and that both Nap1 and Vps75 interact with the RNA polymerase II kinase, CTK1. Loss of NAP1 or VPS75 suppressed cryptic transcription within the open reading frame (ORF) observed when strains are deleted for the kinase CTK1. Loss of the histone acetyltransferase Rtt109 also suppressed ctk1-dependent cryptic transcription. Vps75 regulates Rtt109 function, suggesting that they function together in this process. Histone H3 K9 was found to be the important lysine that is acetylated by Rtt109 during ctk1-dependent cryptic transcription. We showed that both Vps75 and Nap1 regulate the relative level of H3 K9 acetylation in the STE11 ORF. This supports a model in which Nap1, like Vps75, directly regulates Rtt109 activity or regulates the assembly of acetylated chromatin. Although Nap1 and Vps75 share many similarities, due to their distinct interactions with SET2, Nap1 and Vps75 may also play separate roles during transcription elongation. This work sheds further light on the importance of histone chaperones as general regulators of transcription elongation.

Indexed as

AcetylationChromatin Assembly and DisassemblyHistone AcetyltransferasesHistone ChaperonesHistonesMAP Kinase Kinase KinasesMethyltransferasesMolecular ChaperonesNucleosome Assembly Protein 1Open Reading FramesProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticCTDK-I protein complex, S cerevisiaeHistone AcetyltransferasesHistone ChaperonesHistonesMAP Kinase Kinase KinasesMethyltransferasesMolecular ChaperonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1Protein KinasesRtt109 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSet2 protein, S cerevisiaeSte11 protein, S cerevisiaeVps75 protein, S cerevisiae

Identifiers

PMID23401858
PMCPMC3624251
OpenAlexW2135773343

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.