Evidence map›Paper›PMID 30753618›Full record

ArticleNucleic acids research2019

Structural basis of ubiquitin recognition by the winged-helix domain of Cockayne syndrome group B protein.

Tomio S Takahashi, Yusuke Sato, Atsushi Yamagata, Sakurako Goto-Ito, Masafumi Saijo, Shuya Fukai

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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, 22 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Tomio S TakahashiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Yusuke SatoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Atsushi YamagataInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Sakurako Goto-ItoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Masafumi SaijoGraduate School of Frontier Biosciences, Osaka University, Yamadaoka 1-3, Suita, Osaka 565-0871, Japan.
Shuya FukaiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.
Japan Synchrotron Radiation Research Institute · JPThe University of Osaka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cockayne syndrome group B (CSB, also known as ERCC6) protein is involved in many DNA repair processes and essential for transcription-coupled repair (TCR). The central region of CSB has the helicase motif, whereas the C-terminal region contains important regulatory elements for repair of UV- and oxidative stress-induced damages and double-strand breaks (DSBs). A previous study suggested that a small part (∼30 residues) within this region was responsible for binding to ubiquitin (Ub). Here, we show that the Ub-binding of CSB requires a larger part of CSB, which was previously identified as a winged-helix domain (WHD) and is involved in the recruitment of CSB to DSBs. We also present the crystal structure of CSB WHD in complex with Ub. CSB WHD folds as a single globular domain, defining a class of Ub-binding domains (UBDs) different from 23 UBD classes identified so far. The second α-helix and C-terminal extremity of CSB WHD interact with Ub. Together with structure-guided mutational analysis, we identified the residues critical for the binding to Ub. CSB mutants defective in the Ub binding reduced repair of UV-induced damage. This study supports the notion that DSB repair and TCR may be associated with the Ub-binding of CSB.

Indexed as

DNA Breaks, Double-StrandedAmino Acid SequenceCell SurvivalCockayne SyndromeDNA DamageDNA HelicasesDNA RepairDNA Repair EnzymesHumansMutationPoly-ADP-Ribose Binding ProteinsProtein Conformation, alpha-HelicalUbiquitinUbiquitinsUltraviolet RaysWinged-Helix Transcription FactorsDNA HelicasesDNA Repair EnzymesERCC6 protein, humanPoly-ADP-Ribose Binding ProteinsUbiquitinUbiquitinsWinged-Helix Transcription Factors

Identifiers

PMID30753618
PMCPMC6468306
OpenAlexW2914293655

What OpenQuestion holds

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LicenceCC BY-NC
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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.