Evidence map›Paper›PMID 34585421›Full record

ArticleThe EMBO journal2021

DNA asymmetry promotes SUMO modification of the single-stranded DNA-binding protein RPA.

Laurent Cappadocia, Tomasz Kochańczyk, Christopher D Lima

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  9. Article
  10. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
  11. 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

3 authors at 3 institutions in 2 countries.

Laurent CappadociaStructural Biology Program, Sloan Kettering Institute, New York, NY, USA.ORCID 0000-0001-7348-1982
Tomasz KochańczykStructural Biology Program, Sloan Kettering Institute, New York, NY, USA.ORCID 0000-0002-4989-8064
Christopher D LimaStructural Biology Program, Sloan Kettering Institute, New York, NY, USA.ORCID 0000-0002-9163-6092
Howard Hughes Medical Institute · USKettering University · USUniversité du Québec à Montréal · CA

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural studies of RNA processing and ubiquitin-like protein modificationR35GM118080 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI CHRISTOPHER D. LIMA · 2016 to 2026
$5.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA008748NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R35 GM118080
6 · The paper itself

Abstract

Repair of DNA double-stranded breaks by homologous recombination (HR) is dependent on DNA end resection and on post-translational modification of repair factors. In budding yeast, single-stranded DNA is coated by replication protein A (RPA) following DNA end resection, and DNA-RPA complexes are then SUMO-modified by the E3 ligase Siz2 to promote repair. Here, we show using enzymatic assays that DNA duplexes containing 3' single-stranded DNA overhangs increase the rate of RPA SUMO modification by Siz2. The SAP domain of Siz2 binds DNA duplexes and makes a key contribution to this process as highlighted by models and a crystal structure of Siz2 and by assays performed using protein mutants. Enzymatic assays performed using DNA that can accommodate multiple RPA proteins suggest a model in which the SUMO-RPA signal is amplified by successive rounds of Siz2-dependent SUMO modification of RPA and dissociation of SUMO-RPA at the junction between single- and double-stranded DNA. Our results provide insights on how DNA architecture scaffolds a substrate and E3 ligase to promote SUMO modification in the context of DNA repair.

Indexed as

Crystallography, X-RayDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedFluorescence PolarizationMutationNucleic Acid HeteroduplexesProtein DomainsReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitin-Protein LigasesDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedNucleic Acid HeteroduplexesReplication Protein ARFA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSiz1 protein, S cerevisiaeSiz2 protein, S cerevisiaeSmall Ubiquitin-Related Modifier ProteinsSMT3 protein, S cerevisiaeUbiquitin-Protein LigasesE3 ligasehomologous recombinationpost-translational modificationreplication protein Asmall ubiquitin-like modifier

Identifiers

PMID34585421
PMCPMC8591536
OpenAlexW3202111929

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.