Evidence map›Paper›PMID 18498648›Full record

ArticleRetrovirology2008

Lysine methylation of HIV-1 Tat regulates transcriptional activity of the viral LTR.

Rachel Van Duyne, Rebecca Easley, Weilin Wu, Reem Berro, Caitlin Pedati, Zachary Klase, Kylene Kehn-Hall, Elizabeth K Flynn, David E Symer, Fatah Kashanchi

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

56 citing papers in PubMed, 83 citations in OpenAlex.

  1. The Many Faces of SetDB1.Epigenomes · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Targets of histone H3 lysine 9 methyltransferases.Frontiers in cell and developmental biology · 2022
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Genetic variation and function of the HIV-1 Tat protein.Medical microbiology and immunology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

10 authors at 4 institutions in 1 country.

Rachel Van DuyneThe George Washington University Medical Center, Department of Biochemistry and Molecular Biology, Washington, DC 20037, USA. bcmrvv@gwumc.edu
Rebecca Easley
Weilin Wu
Reem Berro
Caitlin Pedati
Zachary Klase
Kylene Kehn-Hall
Elizabeth K Flynn
David E Symer
Fatah Kashanchi
George Washington University · USWashington University Medical Center · USCenter for Cancer Research · USNational Cancer Institute · US

Funding

Characterization of candidate histone methyltransferasesZ01BC010631 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SYMER, DAVID ERIC · 2004 to 2008
$593k
A human stem cell mouse model for HIV expression and inhibitionR21AI071903 · NIAID · GEORGE WASHINGTON UNIVERSITY · PI KASHANCHI, FATAH · 2006 to 2007
$415k
Intramural NIH HHS NIH0011255384Intramural NIH HHS Z01 BC010631NIAID NIH HHS AI071903-01NIAID NIH HHS R21 AI071903
6 · The paper itself

Abstract

backgroundThe rate of transcription of the HIV-1 viral genome is mediated by the interaction of the viral protein Tat with the LTR and other transcriptional machinery. These specific interactions can be affected by the state of post-translational modifications on Tat. Previously, we have shown that Tat can be phosphorylated and acetylated in vivo resulting in an increase in the rate of transcription. In the present study, we investigated whether Tat could be methylated on lysine residues, specifically on lysine 50 and 51, and whether this modification resulted in a decrease of viral transcription from the LTR.

resultsWe analyzed the association of Tat with histone methyltransferases of the SUV39-family of SET domain containing proteins in vitro. Tat was found to associate with both SETDB1 and SETDB2, two enzymes which exhibit methyltransferase activity. siRNA against SETDB1 transfected into cell systems with both transient and integrated LTR reporter genes resulted in an increase in transcription of the HIV-LTR in the presence of suboptimal levels of Tat. In vitro methylation assays with Tat peptides containing point mutations at lysines 50 and 51 showed an increased incorporation of methyl groups on lysine 51, however, both residues indicated susceptibility for methylation.

conclusionThe association of Tat with histone methyltransferases and the ability for Tat to be methylated suggests an interesting mechanism of transcriptional regulation through the recruitment of chromatin remodeling proteins to the HIV-1 promoter.

Indexed as

HIV Long Terminal RepeatTranscription, GeneticCell LineGenes, ReporterHistone-Lysine N-MethyltransferaseHIV-1HumansLysineMethylationProtein BindingProtein MethyltransferasesProtein Processing, Post-TranslationalProtein Structure, TertiaryRNA, Small Interferingtat Gene Products, Human Immunodeficiency VirusTranscriptional ActivationHistone-Lysine N-MethyltransferaseLysineProtein MethyltransferasesRNA, Small InterferingSETDB1 protein, humantat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID18498648
PMCPMC2412914
OpenAlexW2135048849

What OpenQuestion holds

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LicenceCC BY
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.