Evidence map›Paper›PMID 30357414›Full record

ArticleNucleic acids research2018

Structural insights into the duplex DNA processing of TREX2.

Hiu-Lo Cheng, Chun-Ting Lin, Kuan-Wei Huang, Shuying Wang, Yeh-Tung Lin, Shu-Ing Toh, Yu-Yuan Hsiao

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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  14. Statistical learning of protein elastic network from positional covariance matrix.Computational and structural biotechnology journal · 2023
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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 2 institutions in 1 country.

Hiu-Lo ChengInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan 30050, ROC.
Chun-Ting LinDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC.
Kuan-Wei HuangDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC.
Shuying WangDepartment of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan 70101, ROC.
Yeh-Tung LinDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC.
Shu-Ing TohDepartment of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan 30068, ROC.
Yu-Yuan HsiaoInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan 30050, ROC.
National Yang Ming Chiao Tung University · TWNational Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The three prime repair exonuclease 2 (TREX2) is an essential 3'-to-5' exonuclease that functions in cell proliferation, genome integrity and skin homeostasis maintenance. The abnormal expression level of TREX2 can result in broken chromosome, increased susceptibility to skin carcinogenesis and Psoriasis. However, the molecular mechanisms of how TREX2 binds and processes its natural substrates, dsDNA or chromosomal DNA, to maintain genome stability remain unclear. In this study, we present four new crystal structures: apo-TREX2, TREX2 in complex with two different dsDNA substrates, and TREX2 in complex with a processed dsDNA product. Analysis of the structures reveals that TREX2 stacks with the 5'-terminal of dsDNA by a Leu20-Pro21-Asn22 cluster for precisely trimming the 3'-overhang. In addition, TREX2 specifically interacts with the non-scissile strand of dsDNA by an α-helix-loop region. The unique interaction patterns of the TREX2-dsDNA complex highlight the requirement of long double-stranded region for TREX2 binding and provide evidence of the functional role of TREX2 in processing chromosomal DNA. Moreover, the non-processive property of TREX2 is elucidated by the structure of TREX2-product complex. Our work discloses the first structural basis of the molecular interactions between TREX2 and its substrates and unravels the mechanistic actions of TREX2.

Indexed as

Amino Acid MotifsAnimalsApoproteinsCatalytic DomainCloning, MolecularCrystallography, X-RayDNAEscherichia coliExodeoxyribonucleasesGene ExpressionGenetic VectorsMiceModels, MolecularNucleic Acid ConformationProtein BindingProtein Conformation, alpha-HelicalApoproteinsDNAExodeoxyribonucleasesProtein SubunitsRecombinant ProteinsTrex2 protein, mouse

Identifiers

PMID30357414
PMCPMC6294518
OpenAlexW2898221730

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.