Evidence map›Paper›PMID 33589610›Full record

ArticleNature communications2021

HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones.

Fa-Hui Sun, Peng Zhao, Nan Zhang, Lu-Lu Kong, Catherine C L Wong, Cai-Hong Yun

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
5.6field-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

53 citing papers in PubMed, 85 citations in OpenAlex.

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  4. 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

6 authors at 1 institution in 1 country.

Fa-Hui Sun *Department of Biochemistry and Biophysics, Peking University Health Science Center, Beijing, China.
Peng Zhao *Department of Biochemistry and Biophysics, Peking University Health Science Center, Beijing, China.
Nan ZhangSchool of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Lu-Lu KongDepartment of Biochemistry and Biophysics, Peking University Health Science Center, Beijing, China.
Catherine C L WongSchool of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID 0000-0002-6855-2798
Cai-Hong YunDepartment of Biochemistry and Biophysics, Peking University Health Science Center, Beijing, China. yunch@pku.edu.cn.ORCID 0000-0002-5880-8307
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Upon binding to DNA breaks, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other factors to initiate DNA repair. Serine is the major residue for ADP-ribosylation upon DNA damage, which strictly depends on HPF1. Here, we report the crystal structures of human HPF1/PARP1-CAT ΔHD complex at 1.98 Å resolution, and mouse and human HPF1 at 1.71 Å and 1.57 Å resolution, respectively. Our structures and mutagenesis data confirm that the structural insights obtained in a recent HPF1/PARP2 study by Suskiewicz et al. apply to PARP1. Moreover, we quantitatively characterize the key residues necessary for HPF1/PARP1 binding. Our data show that through salt-bridging to Glu284/Asp286, Arg239 positions Glu284 to catalyze serine ADP-ribosylation, maintains the local conformation of HPF1 to limit PARP1 automodification, and facilitates HPF1/PARP1 binding by neutralizing the negative charge of Glu284. These findings, along with the high-resolution structural data, may facilitate drug discovery targeting PARP1.

Indexed as

ADP-RibosylationAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCloning, MolecularCrystallography, X-RayDNAEscherichia coliGene ExpressionGenetic VectorsGlutamineHistonesHumansMiceModels, MolecularCarrier ProteinsDNAGlutamineHistonesHPF1 protein, humanNuclear ProteinsPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Protein IsoformsRecombinant ProteinsSerine

Identifiers

PMID33589610
PMCPMC7884425
OpenAlexW3130199528

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.