Evidence map›Paper›PMID 26743002›Full record

ArticleNucleic acids research2016

S. cerevisiae Mre11 recruits conjugated SUMO moieties to facilitate the assembly and function of the Mre11-Rad50-Xrs2 complex.

Yu-Jie Chen, Yu-Chien Chuang, Chi-Ning Chuang, Yun-Hsin Cheng, Chuang-Rung Chang, Chih-Hsiang Leng, Ting-Fang Wang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.4field-weighted citation impact, top 11% 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, 28 citations in OpenAlex.

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  4. Advances in SUMO-based regulation of homologous recombination.Current opinion in genetics & development · 2021
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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

7 authors at 3 institutions in 1 country.

Yu-Jie ChenGraduate Program of Biotechnology in Medicine, National Tsing Hua University and National Health Research Institutes, Taiwan Institute of Biotechnology, National Tsing Hua University, Hsinchu 300, Taiwan National Institute of Infectious Diseases and Vaccinology, National Health Research Institute, Miaoli 350, Taiwan Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Yu-Chien ChuangInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Chi-Ning ChuangInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Yun-Hsin ChengInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Chuang-Rung ChangGraduate Program of Biotechnology in Medicine, National Tsing Hua University and National Health Research Institutes, Taiwan Institute of Biotechnology, National Tsing Hua University, Hsinchu 300, Taiwan.
Chih-Hsiang LengGraduate Program of Biotechnology in Medicine, National Tsing Hua University and National Health Research Institutes, Taiwan National Institute of Infectious Diseases and Vaccinology, National Health Research Institute, Miaoli 350, Taiwan tfwang@gate.sinica.edu.tw.
Ting-Fang WangInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan tfwang@gate.sinica.edu.tw.
Institute of Molecular Biology, Academia Sinica · TWNational Health Research Institutes · TWNational Tsing Hua University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Double-strand breaks (DSBs) in chromosomes are the most challenging type of DNA damage. The yeast and mammalian Mre11-Rad50-Xrs2/Nbs1 (MRX/N)-Sae2/Ctp1 complex catalyzes the resection of DSBs induced by secondary structures, chemical adducts or covalently-attached proteins. MRX/N also initiates two parallel DNA damage responses-checkpoint phosphorylation and global SUMOylation-to boost a cell's ability to repair DSBs. However, the molecular mechanism of this SUMO-mediated response is not completely known. In this study, we report that Saccharomyces cerevisiae Mre11 can non-covalently recruit the conjugated SUMO moieties, particularly the poly-SUMO chain. Mre11 has two evolutionarily-conserved SUMO-interacting motifs, Mre11(SIM1) and Mre11(SIM2), which reside on the outermost surface of Mre11. Mre11(SIM1) is indispensable for MRX assembly. Mre11(SIM2) non-covalently links MRX with the SUMO enzymes (E2/Ubc9 and E3/Siz2) to promote global SUMOylation of DNA repair proteins. Mre11(SIM2) acts independently of checkpoint phosphorylation. During meiosis, the mre11(SIM2) mutant, as for mre11S, rad50S and sae2Δ, allows initiation but not processing of Spo11-induced DSBs. Using MRX and DSB repair as a model, our work reveals a general principle in which the conjugated SUMO moieties non-covalently facilitate the assembly and functions of multi-subunit protein complexes.

Indexed as

DNA RepairGene Expression Regulation, FungalDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA, FungalEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMeiosisMeiotic Recombination Protein SPO11Models, MolecularPhosphorylationProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsDNA, FungalEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMeiotic Recombination Protein SPO11MRE11 protein, S cerevisiaeRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeSiz2 protein, S cerevisiaeSpo11 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9XRS2 protein, S cerevisiae

Identifiers

PMID26743002
PMCPMC4797280
OpenAlexW2229855034

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.