T
Takeshi Chujo
Researcher at Kumamoto University
Publications - 24
Citations - 1710
Takeshi Chujo is an academic researcher from Kumamoto University. The author has contributed to research in topics: RNA & Transfer RNA. The author has an hindex of 10, co-authored 18 publications receiving 1229 citations. Previous affiliations of Takeshi Chujo include Hokkaido University & University of Tokyo.
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Journal ArticleDOI
Functional Domains of NEAT1 Architectural lncRNA Induce Paraspeckle Assembly through Phase Separation.
Tomohiro Yamazaki,Sylvie Souquere,Takeshi Chujo,Simon Kobelke,Yee Seng Chong,Archa H. Fox,Charles S. Bond,Shinichi Nakagawa,Gérard Pierron,Tetsuro Hirose +9 more
TL;DR: It is demonstrated that the enrichment of NONO dimers on the redundant NEAT1_2 subdomains initiates construction of phase-separated paraspeckles, providing mechanistic insights into lncRNA-based nuclear body formation.
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The TDRD9-MIWI2 complex is essential for piRNA-mediated retrotransposon silencing in the mouse male germline.
Masanobu Shoji,Takashi Tanaka,Mihoko Hosokawa,Michael Reuter,Alexander Stark,Yuzuru Kato,Gen Kondoh,Katsuya Okawa,Takeshi Chujo,Tsutomu Suzuki,Kenichiro Hata,Sandra L. Martin,Toshiaki Noce,Satomi Kuramochi-Miyagawa,Toru Nakano,Hiroyuki Sasaki,Ramesh S. Pillai,Norio Nakatsuji,Shinichiro Chuma +18 more
TL;DR: It is shown that tudor-domain containing 9 (Tdrd9) is essential for silencing Line-1 retrotransposon in the mouse male germline, and the results identify TDRD9 as a functional partner of MIWI2 and indicate that the tUDor-piwi association is a conserved feature.
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Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization
Jason A. West,Mari Mito,Satoshi Kurosaka,Toru Takumi,Chiharu Tanegashima,Takeshi Chujo,Kaori Yanaka,Robert E. Kingston,Tetsuro Hirose,Charles S. Bond,Archa H. Fox,Archa H. Fox,Shinichi Nakagawa +12 more
TL;DR: Using structural illumination microscopy, West et al. show that paraspeckle proteins are arranged around bundles of Neat1, forming core-shell spheroidal structures dependent on the RNA binding protein Fus.
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LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria
Takeshi Chujo,Takayuki Ohira,Yuriko Sakaguchi,Naoki Goshima,Nobuo Nomura,Asuteka Nagao,Tsutomu Suzuki +6 more
TL;DR: This work observed that the LRPPRC/SLIRP complex suppressed 3′ exonucleolytic mRNA degradation mediated by PNPase and SUV3, and promoted the polyadenylation of mRNAs mediated by mitochondrial poly(A) polymerase (MTPAP) in vitro.
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Architectural RNAs (arcRNAs): A class of long noncoding RNAs that function as the scaffold of nuclear bodies.
TL;DR: A class of lncRNAs termed architectural RNAs (arcRNAs) that function as the essential scaffold or platform of nuclear bodies that sequestrate specific regulatory proteins, thereby changing gene expression patterns are defined.