Evidence map›Paper›PMID 33067435›Full record

ArticleNature communications2020

Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry.

Alexandra Stützer, Luisa M Welp, Monika Raabe, Timo Sachsenberg, Christin Kappert, Alexander Wulf, Andy M Lau, Stefan-Sebastian David, Aleksandar Chernev, Katharina Kramer and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.8field-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

30 citing papers in PubMed, 43 citations in OpenAlex.

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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

14 authors at 6 institutions in 3 countries.

Alexandra StützerBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Luisa M WelpBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Monika RaabeBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Timo SachsenbergInstitute for Bioinformatics and Medical Informatics, University of Tübingen, 72076, Tübingen, Germany.ORCID 0000-0002-2833-6070
Christin KappertBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Alexander WulfBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Andy M LauDepartment of Chemistry, King's College London, London, SE1 1DB, UK.ORCID 0000-0003-0572-7826
Stefan-Sebastian DavidLaboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Aleksandar ChernevBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Katharina KramerCSL Behring GmbH, 35041, Marburg, Germany.
Argyris PolitisDepartment of Chemistry, King's College London, London, SE1 1DB, UK.ORCID 0000-0002-1617-4238
Oliver KohlbacherInstitute for Bioinformatics and Medical Informatics, University of Tübingen, 72076, Tübingen, Germany.ORCID 0000-0003-1739-4598
Wolfgang FischleLaboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany. henning.urlaub@mpibpc.mpg.de.ORCID 0000-0003-1837-5233
Max Planck Institute for Biophysical Chemistry · DEKing's College London · GBBehringwerke (Germany) · DEMax Planck Institute for Developmental Biology · DEUniversitätsmedizin Göttingen · DEUniversity of Tübingen · DE

Funding

Medical Research CouncilWellcome TrustWellcome Trust 109854/Z/15/Z
6 · The paper itself

Abstract

Protein-DNA interactions are key to the functionality and stability of the genome. Identification and mapping of protein-DNA interaction interfaces and sites is crucial for understanding DNA-dependent processes. Here, we present a workflow that allows mass spectrometric (MS) identification of proteins in direct contact with DNA in reconstituted and native chromatin after cross-linking by ultraviolet (UV) light. Our approach enables the determination of contact interfaces at amino-acid level. With the example of chromatin-associated protein SCML2 we show that our technique allows differentiation of nucleosome-binding interfaces in distinct states. By UV cross-linking of isolated nuclei we determined the cross-linking sites of several factors including chromatin-modifying enzymes, demonstrating that our workflow is not restricted to reconstituted materials. As our approach can distinguish between protein-RNA and DNA interactions in one single experiment, we project that it will be possible to obtain insights into chromatin and its regulation in the future.

Indexed as

ChromatinDNAHumansMass SpectrometryNucleosomesPolycomb-Group ProteinsProtein BindingProteinsUltraviolet RaysChromatinDNANucleosomesPolycomb-Group ProteinsProteinsSCML2 protein, human

Identifiers

PMID33067435
PMCPMC7567871
OpenAlexW3092934328

What OpenQuestion holds

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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.