Evidence map›Paper›PMID 38307862›Full record

ArticleNature communications2024

Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1.

Luka Bacic, Guillaume Gaullier, Jugal Mohapatra, Guanzhong Mao, Klaus Brackmann, Mikhail Panfilov, Glen Liszczak, Anton Sabantsev, Sebastian Deindl

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. 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
5.4field-weighted citation impact, top 3% 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, 19 citations in OpenAlex.

  1. Article
  2. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
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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

9 authors at 2 institutions in 2 countries.

Luka BacicDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden.
Guillaume GaullierDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden.ORCID 0000-0003-3405-6021
Jugal MohapatraDepartment of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX, 75390, USA.
Guanzhong MaoDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden.
Klaus BrackmannDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden.
Mikhail PanfilovDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden.ORCID 0000-0003-2875-7315
Glen LiszczakDepartment of Biochemistry, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX, 75390, USA.
Anton SabantsevDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden. anton.sabantcev@icm.uu.se.ORCID 0000-0002-8559-8894
Sebastian DeindlDepartment of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, 75124, Uppsala, Sweden. sebastian.deindl@icm.uu.se.ORCID 0000-0001-6807-8654
Uppsala University · SEThe University of Texas Southwestern Medical Center · US

Funding

Regulation and function of site-specific protein poly-ADP-ribosylationR35GM147140 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Glen Liszczak · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM147140
6 · The paper itself

Abstract

The chromatin remodeler ALC1 is activated by DNA damage-induced poly(ADP-ribose) deposited by PARP1/PARP2 and their co-factor HPF1. ALC1 has emerged as a cancer drug target, but how it is recruited to ADP-ribosylated nucleosomes to affect their positioning near DNA breaks is unknown. Here we find that PARP1/HPF1 preferentially initiates ADP-ribosylation on the histone H2B tail closest to the DNA break. To dissect the consequences of such asymmetry, we generate nucleosomes with a defined ADP-ribosylated H2B tail on one side only. The cryo-electron microscopy structure of ALC1 bound to such an asymmetric nucleosome indicates preferential engagement on one side. Using single-molecule FRET, we demonstrate that this asymmetric recruitment gives rise to directed sliding away from the DNA linker closest to the ADP-ribosylation site. Our data suggest a mechanism by which ALC1 slides nucleosomes away from a DNA break to render it more accessible to repair factors.

Indexed as

NucleosomesPoly ADP RibosylationChromatinCryoelectron MicroscopyDNA BreaksDNA RepairPoly (ADP-Ribose) Polymerase-1ChromatinNucleosomesPoly (ADP-Ribose) Polymerase-1

Identifiers

PMID38307862
PMCPMC10837151
OpenAlexW4391471287

What OpenQuestion holds

Textmetadata
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.