Mengxi Wang

Shaanxi University of Science and Technology

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Guang Yang

Chongqing University of Science and Technology

Xiuhua Liu

Hebei University

Chen Wu

Hebei University

Muzaffer Ahmad Kassab

City of Hope

Fabio Spada

Guy's and St Thomas' NHS Foundation Trust

Weihua Qin

North University of China

Jiaxu Wang

Chinese PLA General Hospital

Yinliang Ma

Hebei University

Zenglin Yuan

Shandong University

Yaqi Cui

First Affiliated Hospital of Zhengzhou University

Cooperative Institutions

Ludwig-Maximilians-Universität München

Center for Integrated Protein Science Munich

Chinese Academy of Sciences

Nanjing Agricultural University

University of Chinese Academy of Sciences

University of Science and Technology Beijing

University of Massachusetts Chan Medical School

City of Hope

Cancer Genetics (United States)

Beckman Research Institute

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Intrinsic and Extrinsic Connections of Tet3 Dioxygenase with CXXC Zinc Finger Modules

PLoS ONE (2013)

Nan Liu Mengxi Wang Wen Deng Christine S. Schmidt Weihua Qin

Tet proteins are emerging as major epigenetic modulators of cell fate and plasticity. However, little is known about how Tet proteins are targeted to selected genomic loci in distinct biological contexts. Previously, a CXXC-type zinc finger domain in Tet1 was shown to bind CpG-rich DNA sequences. Interestingly, in human and mouse the Tet2 and Tet3 genes are adjacent to Cxxc4 and Cxxc10-1, respectively. The CXXC domains encoded by these loci, together with those in Tet1 and Cxxc5, identify a distinct homology group within the CXXC domain family. Here we provide evidence for alternative mouse Tet3 transcripts including the Cxxc10-1 sequence (Tet3CXXC) and for an interaction between Tet3 and Cxxc4. In vitro Cxxc4 and the isolated CXXC domains of Tet1 and Tet3CXXC bind DNA substrates with similar preference towards the modification state of cytosine at a single CpG site. In vivo Tet1 and Tet3 isoforms with and without CXXC domain hydroxylate genomic 5-methylcytosine with similar activity. Relative transcript levels suggest that distinct ratios of Tet3CXXC isoforms and Tet3-Cxxc4 complex may be present in adult tissues. Our data suggest that variable association with CXXC modules may contribute to context specific functions of Tet proteins.

CpG site

5-Methylcytosine

genomic DNA

PHD finger

10.1371/journal.pone.0062755

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Citations (42)

Author Correction: Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR

Nature Communications (2019)

Jiaxu Wang Zenglin Yuan Yaqi Cui Rong Xie Guang Yang

The original version of this Article contained an error in the author affiliations. Xiaochun Yu was incorrectly associated with College of Life Sciences, Hebei University, Baoding 071000 Hebei, China.This has now been corrected in both the PDF and HTML versions of the Article.

10.1038/s41467-018-08086-w

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Genesis of LCT Pegmatites during Early Paleozoic Orogeny of the North Qinling Orogenic Belt, China: Emplacement Conditions and Structural Control

Acta Geologica Sinica - English Edition (2024)

Jubiao Cen Yonggang Feng Ting Liang Mengxi Wang Jianxin Zhang

Abstract The Guanpo pegmatite field in the North Qinling orogenic belt (NQB), China, hosts the most abundant LCT pegmatites. However, their emplacement conditions and structural control remain unexplored. In this contribution, we investigated it combining pegmatite orientation measurement with oxygen isotope geothermometry and fluid inclusion study. The orientations of type A1 pegmatites (P f < σ 2 ) are predominantly influenced by P‐ and T‐fractures due to simple shearing in Shiziping dextral thrust shear zone during D 2 deformation, whereas type A2 pegmatites (contemporaneous with D 4 ) are governed by hydraulic fractures aligned with S 0 and S 0+ 1 stemming from fluid pressure (P f <σ 2 ) . Additionally, type B pegmatites ( P f ≤ σ 2 ) exhibit orientations shaped by en echelon extensional fractures in local ductile shear zones (contemporaneous with D 3 ). The albite‐quartz oxygen isotope geothermometry and microthermometric analysis of fluid inclusions in elbaites from the latest pegmatites (including types B and A2) suggest that the crystallization P‐T for late magmatic and hydrothermal stages are 527.5–559.2°C, 320°C, 3.1–3.6 kbar and 2.0 kbar, respectively. Our observations along with previous studies suggest that the genesis of the LCT pegmatites was a long‐term, multi‐stage event during early Paleozoic orogeny (including the collision stage) of the NQB, and was facilitated by various local fractures.

Pegmatite

Orogeny

10.1111/1755-6724.15179

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Different Binding Properties and Function of CXXC Zinc Finger Domains in Dnmt1 and Tet1

PLoS ONE (2011)

Carina Frauer Andrea Rottach Daniela Meilinger Sebastian Bultmann Karin Fellinger

Several mammalian proteins involved in chromatin and DNA modification contain CXXC zinc finger domains. We compared the structure and function of the CXXC domains in the DNA methyltransferase Dnmt1 and the methylcytosine dioxygenase Tet1. Sequence alignment showed that both CXXC domains have a very similar framework but differ in the central tip region. Based on the known structure of a similar MLL1 domain we developed homology models and designed expression constructs for the isolated CXXC domains of Dnmt1 and Tet1 accordingly. We show that the CXXC domain of Tet1 has no DNA binding activity and is dispensable for catalytic activity in vivo. In contrast, the CXXC domain of Dnmt1 selectively binds DNA substrates containing unmethylated CpG sites. Surprisingly, a Dnmt1 mutant construct lacking the CXXC domain formed covalent complexes with cytosine bases both in vitro and in vivo and rescued DNA methylation patterns in dnmt1−/− embryonic stem cells (ESCs) just as efficiently as wild type Dnmt1. Interestingly, neither wild type nor ΔCXXC Dnmt1 re-methylated imprinted CpG sites of the H19a promoter in dnmt1−/− ESCs, arguing against a role of the CXXC domain in restraining Dnmt1 methyltransferase activity on unmethylated CpG sites.

DNMT1

CpG site

DNA methyltransferase

10.1371/journal.pone.0016627

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Citations (95)

Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR

Nature Communications (2018)

Jiaxu Wang Zenglin Yuan Yaqi Cui Rong Xie Guang Yang

53BP1 performs essential functions in DNA double-strand break (DSB) repair and it was recently reported that Tudor interacting repair regulator (TIRR) negatively regulates 53BP1 during DSB repair. Here, we present the crystal structure of the 53BP1 tandem Tudor domain (TTD) in complex with TIRR. Our results show that three loops from TIRR interact with 53BP1 TTD and mask the methylated lysine-binding pocket in TTD. Thus, TIRR competes with histone H4K20 methylation for 53BP1 binding. We map key interaction residues in 53BP1 TTD and TIRR, whose mutation abolishes complex formation. Moreover, TIRR suppresses the relocation of 53BP1 to DNA lesions and 53BP1-dependent DNA damage repair. Finally, despite the high-sequence homology between TIRR and NUDT16, NUDT16 does not directly interact with 53BP1 due to the absence of key residues required for binding. Taken together, our study provides insights into the molecular mechanism underlying TIRR-mediated suppression of 53BP1-dependent DNA damage repair.

10.1038/s41467-018-05174-9

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Citations (23)

Orally delivered siRNA targeting macrophage Map4k4 suppresses systemic inflammation

Nature (2009)

Myriam Aouadi Gregory J. Tesz Sarah M. Nicoloro Mengxi Wang My Chouinard

Systemic administration

10.1038/nature07774

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Citations (548)

Improving the activity and expression level of a phthalate-degrading enzyme by a combination of mutagenesis strategies and strong promoter replacement

Environmental Science and Pollution Research (2023)

Shengwei Sun Yuzhi Tan Luyao Wang Zichao Wu Jingjie Zhou

Enzyme Kinetics

Saturated mutagenesis

Phthalic acid

Site-directed mutagenesis

Dibutyl phthalate

10.1007/s11356-023-25263-7

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Citations (3)

Conductive, adhesive, and biocompatible hydrogel sensor based on zwitterionic for effective wound healing and monitoring

Chemical Engineering Journal (2025)

Meng Wei Haihua Wang Chaoxian Chen Guiqiang Fei Dong Yang

Biocompatible material

10.1016/j.cej.2025.160235

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Field-free spin-orbit torque switching via out-of-plane spin-polarization induced by an antiferromagnetic insulator/heavy metal interface

Nature Communications (2023)

Mengxi Wang Jun Zhou Xiaoguang Xu Tanzhao Zhang Zhiqiang Zhu

Manipulating spin polarization orientation is challenging but crucial for field-free spintronic devices. Although such manipulation has been demonstrated in a limited number of antiferromagnetic metal-based systems, the inevitable shunting effects from the metallic layer can reduce the overall device efficiency. In this study, we propose an antiferromagnetic insulator-based heterostructure NiO/Ta/Pt/Co/Pt for such spin polarization control without any shunting effect in the antiferromagnetic layer. We show that zero-field magnetization switching can be realized and is related to the out-of-plane component of spin polarization modulated by the NiO/Pt interface. The zero-field magnetization switching ratio can be effectively tuned by the substrates, in which the easy axis of NiO can be manipulated by the tensile or compressive strain from the substrates. Our work demonstrates that the insulating antiferromagnet based heterostructure is a promising platform to enhance the spin-orbital torque efficiency and achieve field-free magnetization switching, thus opening an avenue towards energy-efficient spintronic devices.

10.1038/s41467-023-38550-1

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Citations (28)