Evidence map›Paper›PMID 21606491›Full record

ArticleThe Journal of biological chemistry2011

Autoacetylation of the histone acetyltransferase Rtt109.

Brittany N Albaugh, Kevin M Arnold, Susan Lee, John M Denu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.6field-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

44 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  10. Article
  11. Mechanism of activation for the sirtuin 6 protein deacylase.The Journal of biological chemistry · 2020
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. KATapulting toward Pluripotency and Cancer.Journal of molecular biology · 2017
    Review
  17. Article
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Brittany N AlbaughDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53715, USA.
Kevin M Arnold
Susan Lee
John M Denu
University of Wisconsin–Madison · US

Funding

Molecular mechanisms of histone modification - Alzheimer’s supplement NOT-AG-18-008R37GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2013 to 2022
$3.7M
Molecular Mechanisms of Histone AcetyltransferasesR01GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 1999 to 2012
$2.9M
NIGMS NIH HHS GM059785NIGMS NIH HHS R01 GM059785NIGMS NIH HHS R37 GM059785
6 · The paper itself

Abstract

Rtt109 is a yeast histone acetyltransferase (HAT) that associates with histone chaperones Asf1 and Vps75 to acetylate H3K56, H3K9, and H3K27 and is important in DNA replication and maintaining genomic integrity. Recently, mass spectrometry and structural studies of Rtt109 have shown that active site residue Lys-290 is acetylated. However, the functional role of this modification and how the acetyl group is added to Lys-290 was unclear. Here, we examined the mechanism of Lys-290 acetylation and found that Rtt109 catalyzes intramolecular autoacetylation of Lys-290 ∼200-times slower than H3 acetylation. Deacetylated Rtt109 was prepared by reacting with a sirtuin protein deacetylase, producing an enzyme with negligible HAT activity. Autoacetylation of Rtt109 restored full HAT activity, indicating that autoacetylation is necessary for HAT activity and is a fully reversible process. To dissect the mechanism of activation, biochemical, and kinetic analyses were performed with Lys-290 variants of the Rtt109-Vps75 complex. We found that autoacetylation of Lys-290 increases the binding affinity for acetyl-CoA and enhances the rate of acetyl-transfer onto histone substrates. This study represents the first detailed investigation of a HAT enzyme regulated by single-site intramolecular autoacetylation.

Indexed as

AcetylationEnzyme ActivationHistone AcetyltransferasesMolecular ChaperonesMultiprotein ComplexesProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSirtuinsHistone AcetyltransferasesMolecular ChaperonesMultiprotein ComplexesRtt109 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSirtuinsVps75 protein, S cerevisiae

Identifiers

PMID21606491
PMCPMC3137045
OpenAlexW2067903414

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.