Active DNA unwinding and transport by a membrane-adapted helicase nanopore

Sun, Kai; Zhao, Chengli; Zeng, Xiaojun; Chen, Yuejia; Jiang, Xin; Li, Yiyang; Gou, Lu; Xie, Haiyang; Li, Xinqiong; Zhang, Xialin; Lin, Sheng; Dou, Linqin; Wei, Long; Niu, Haofu; Zhang, Ming; Tian, Ruocen; Sawyer, Erica; Yuan, Qingyue; Huang, Yang; Chen, Piaopiao; Zhao, Chengjian; Zhou, Cuisong; Ying, Binwu; Shi, Bingyang; Wei, Xiawei; Jiang, Ruotian; Zhang, Lei; Lu, Guangwen; Geng, Jia

doi:10.1038/s41467-019-13047-y

Cited by 26 publications

(18 citation statements)

References 54 publications

(69 reference statements)

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“…Although TMEM120A shows the ability to permeate ions as measured in bilayer system, our results indicate TMEM120A does not response to poking or stretch mechanical stimuli in heterologous expression system. We even cannot conclude TMEM120A is an ion channel as conducting currents were also measured for several non-channel proteins in bilayer system 17 . The structural similarity between TMEM120A and ELOVL7, and the extra density bound in the cytosol-facing cavity suggest that TMEM120A may function as an enzyme in lipid metabolism 3 .…”

Section: Discussionmentioning

confidence: 86%

Cryo-EM structures of human TMEM120A and TMEM120B

Zhao

et al. 2021

Preprint

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TMEM120A (Transmembrane protein 120A) was recently identified as a mechanical pain sensing ion channel named as TACAN, while its homologue TMEM120B has no mechanosensing property1. Here, we report the cryo-EM structures of both human TMEM120A and TMEM120B. The two structures share the same dimeric assembly, mediated by extensive interactions through the transmembrane domain (TMD) and the N-terminal coiled coil domain (CCD). However, the nearly identical structures cannot provide clues for the difference in mechanosensing between TMEM120A and TMEM120B. Although TMEM120A could mediate conducting currents in a bilayer system, it does not mediate mechanical-induced currents in a heterologous expression system, suggesting TMEM120A is unlikely a mechanosensing channel. Instead, the TMDs of TMEM120A and TMEM120B resemble the structure of a fatty acid elongase, ELOVL7, indicating their potential role of an enzyme in lipid metabolism.

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Section: Discussionmentioning

confidence: 86%

Cryo-EM structures of human TMEM120A and TMEM120B

Zhao

et al. 2021

Preprint

Self Cite

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show abstract

“…Although TMEM120A shows the ability to permeate ions as measured in bilayer system, our results indicate TMEM120A does not respond to poking or stretch mechanical stimuli in heterologous expression system. We even cannot conclude TMEM120A is an ion channel as conducting currents were also measured for several non-channel proteins in the bilayer system 8 . The structural similarity between TMEM120A and ELOVL7 suggests that TMEM120A may function as an enzyme in lipid metabolism 3 .…”

mentioning

confidence: 88%

Cryo-EM structures of human TMEM120A and TMEM120B

Zhao

et al. 2021

Cell Discov

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“…[ 25 ] Conical nanopores made from glass pipette are fabricated by deformation of materials by external force above their transitional temperature, which has low electric noise, low fabrication cost, robust durability, and the ability to penetrate cell membranes. [ 67–69 ] It has been widely used in protein detection, [ 27,67,70,71 ] and DNA information storage. [ 72 ] (Table 1) Another common method to fabricate conical nanopore is based on current‐feedback chemical etching, which produces sub‐20 nm nanopores on polymer membrane.…”

Section: Fabricationmentioning

confidence: 99%

Four Aspects about Solid‐State Nanopores for Protein Sensing: Fabrication, Sensitivity, Selectivity, and Durability

Tong

Zhao

2020

Adv Healthcare Materials

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Solid‐state nanopores are a mimic of innate biological nanopores embedded on lipid membranes. They are fabricated on thin suspended layers of synthetic materials that provide superior thermal, mechanical, chemical stability, and geometry flexibility. As their counterpart biological nanopores reach the goal of DNA sequencing and become commercial, solid‐state nanopores thrive in aspects of protein sensing and have become an important research component for clinical diagnostic technologies. This review focuses on resistive pulse sensing modes, which are versatile for low‐cost, portable sensing devices and summarizes four main aspects toward commercially available resistive pulse‐based protein sensing techniques using solid‐state nanopores. In each aspect of fabrication, sensitivity, selectivity, and durability, brief fundamentals are introduced and the challenges and improvements are discussed. The rapid advance of a practical technique requires greater multidisciplinary cooperation. The review aims at clarifying existing obstacles in solid‐state nanopore based protein sensing, intriguing readers with existing solutions and finally encouraging multidisciplinary researchers to advance the development of this promising protein sensing methodology.

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Active DNA unwinding and transport by a membrane-adapted helicase nanopore

Cited by 26 publications

References 54 publications

Cryo-EM structures of human TMEM120A and TMEM120B

Cryo-EM structures of human TMEM120A and TMEM120B

Cryo-EM structures of human TMEM120A and TMEM120B

Four Aspects about Solid‐State Nanopores for Protein Sensing: Fabrication, Sensitivity, Selectivity, and Durability

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