Evidence map›Paper›PMID 32366460›Full record

ArticleThe Journal of biological chemistry2020

Histone acetyltransferase 1 is required for DNA replication fork function and stability.

Paula A Agudelo Garcia, Callie M Lovejoy, Prabakaran Nagarajan, Dongju Park, Liudmila V Popova, Michael A Freitas, Mark R Parthun

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Recent insights intoEpigenetics · 2021
    Review
  14. Review
  15. Histone dynamics during DNA replication stress.Journal of biomedical science · 2021
    Review
  16. 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.

Paula A Agudelo GarciaDepartment of Biological Chemistry and Pharmacology, the Ohio State University, Columbus, Ohio, USA.
Callie M LovejoyDepartment of Biological Chemistry and Pharmacology, the Ohio State University, Columbus, Ohio, USA.
Prabakaran NagarajanDepartment of Biological Chemistry and Pharmacology, the Ohio State University, Columbus, Ohio, USA.
Dongju ParkDepartment of Cancer Biology and Genetics, the Ohio State University, Columbus, Ohio, USA.
Liudmila V PopovaDepartment of Biological Chemistry and Pharmacology, the Ohio State University, Columbus, Ohio, USA.
Michael A FreitasDepartment of Cancer Biology and Genetics, the Ohio State University, Columbus, Ohio, USA.
Mark R ParthunDepartment of Biological Chemistry and Pharmacology, the Ohio State University, Columbus, Ohio, USA parthun.1@osu.edu.ORCID 0000-0001-8558-4583
The Ohio State University · US

Funding

Type B Histone Acetyltransferases and the Assembly of Chromatin StructureR01GM062970 · NIGMS · OHIO STATE UNIVERSITY · PI PARTHUN, MARK R · 2001 to 2018
$5.1M
Cellular, molecular, and biochemical sciences training grantT32GM086252 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH, MUSIER-FORSYTH, KARIN M · 2011 to 2020
$2.0M
Ohio State University Neuroscience Center Core-Core EP30NS104177 · NINDS · OHIO STATE UNIVERSITY · PI BROWN, ANTHONY · 2017 to 2020
$1.9M
NIGMS NIH HHS R01 GM062970NIGMS NIH HHS T32 GM086252NINDS NIH HHS P30 NS104177
6 · The paper itself

Abstract

The replisome is a protein complex on the DNA replication fork and functions in a dynamic environment at the intersection of parental and nascent chromatin. Parental nucleosomes are disrupted in front of the replication fork. The daughter DNA duplexes are packaged with an equal amount of parental and newly synthesized histones in the wake of the replication fork through the activity of the replication-coupled chromatin assembly pathway. Histone acetyltransferase 1 (HAT1) is responsible for the cytosolic diacetylation of newly synthesized histone H4 on lysines 5 and 12, which accompanies replication-coupled chromatin assembly. Here, using proximity ligation assay-based chromatin assembly assays and DNA fiber analysis, we analyzed the role of murine HAT1 in replication-coupled chromatin assembly. We demonstrate that HAT1 physically associates with chromatin near DNA replication sites. We found that the association of HAT1 with newly replicated DNA is transient, but can be stabilized by replication fork stalling. The association of HAT1 with nascent chromatin may be functionally relevant, as HAT1 loss decreased replication fork progression and increased replication fork stalling. Moreover, in the absence of HAT1, stalled replication forks were unstable, and newly synthesized DNA became susceptible to MRE11-dependent degradation. These results suggest that HAT1 links replication fork function to the proper processing and assembly of newly synthesized histones.

Indexed as

DNA ReplicationAnimalsCell LineChromatinChromatin Assembly and DisassemblyDNAGene Knockout TechniquesHistone AcetyltransferasesMiceMRE11 Homologue ProteinChromatinDNAHistone AcetyltransferasesMre11a protein, mouseMRE11 Homologue Proteinacetylationacetyltransferasechromatinchromatin assemblyDNA replicationHAT1histone acetylasereplication forkreplication fork stallingreplication stress

Identifiers

PMID32366460
PMCPMC7307201
OpenAlexW3023753358

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.