Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Yuriko Sakaguchi"'
Autor:
Asuteka Nagao, Yui Nakanishi, Yutaro Yamaguchi, Yoshifumi Mishina, Minami Karoji, Takafumi Toya, Tomoya Fujita, Shintaro Iwasaki, Kenjyo Miyauchi, Yuriko Sakaguchi, Tsutomu Suzuki
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-20 (2023)
Abstract In the early stage of bacterial translation, peptidyl-tRNAs frequently dissociate from the ribosome (pep-tRNA drop-off) and are recycled by peptidyl-tRNA hydrolase. Here, we establish a highly sensitive method for profiling of pep-tRNAs usin
Externí odkaz:
https://doaj.org/article/e9718a618adc4f5782970338975e5fd7
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
AtaT is a type-II toxin from enterohemorrhagic E. coli, reported to acetylate the aminoacyl-moiety of initiator Met-tRNAfMet, thus inhibiting translation initiation. Biochemical analysis suggests that AtaT has a broader specificity for aminoacyl-tRNA
Externí odkaz:
https://doaj.org/article/b756a25d8bce42908de151680c466bc3
Autor:
Takeo Suzuki, Yuka Yashiro, Ittoku Kikuchi, Yuma Ishigami, Hironori Saito, Ikuya Matsuzawa, Shunpei Okada, Mari Mito, Shintaro Iwasaki, Ding Ma, Xuewei Zhao, Kana Asano, Huan Lin, Yohei Kirino, Yuriko Sakaguchi, Tsutomu Suzuki
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Mitochondrial tRNA modifications are important for tRNA stability and accurate decoding. By employing RNA mass spectrometry and deep sequencing, here the authors provide a comprehensive analysis of post-transcriptional modifications of 22 species of
Externí odkaz:
https://doaj.org/article/b76731e827284bb38227d56d00e3395f
Autor:
Huan Lin, Kenjyo Miyauchi, Tai Harada, Ryo Okita, Eri Takeshita, Hirofumi Komaki, Kaoru Fujioka, Hideki Yagasaki, Yu-ichi Goto, Kaori Yanaka, Shinichi Nakagawa, Yuriko Sakaguchi, Tsutomu Suzuki
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
Transfer RNA modifications play critical roles in protein synthesis. Here the authors reveal the t6A37 tRNA modification is dynamically regulated by sensing intracellular CO2 concentration in mitochondria, implying metabolic regulation of protein syn
Externí odkaz:
https://doaj.org/article/a003e4e93bed4afa8c4afc18c869c6bf
Autor:
Shigeru Matsuda, Takehiro Yasukawa, Yuriko Sakaguchi, Kenji Ichiyanagi, Motoko Unoki, Kazuhito Gotoh, Kei Fukuda, Hiroyuki Sasaki, Tsutomu Suzuki, Dongchon Kang
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Abstract Whilst 5-methylcytosine (5mC) is a major epigenetic mark in the nuclear DNA in mammals, whether or not mitochondrial DNA (mtDNA) receives 5mC modification remains controversial. Herein, we exhaustively analysed mouse mtDNA using three method
Externí odkaz:
https://doaj.org/article/292dcfe424644832b38fb2830dc1be9a
Autor:
Hiroki Takai, Koji Masuda, Tomohiro Sato, Yuriko Sakaguchi, Takeo Suzuki, Tsutomu Suzuki, Ryo Koyama-Nasu, Yukiko Nasu-Nishimura, Yuki Katou, Haruo Ogawa, Yasuyuki Morishita, Hiroko Kozuka-Hata, Masaaki Oyama, Tomoki Todo, Yasushi Ino, Akitake Mukasa, Nobuhito Saito, Chikashi Toyoshima, Katsuhiko Shirahige, Tetsu Akiyama
Publikováno v:
Cell Reports, Vol 9, Iss 1, Pp 48-60 (2014)
Summary: The development of cancer is driven not only by genetic mutations but also by epigenetic alterations. Here, we show that TET1-mediated production of 5-hydroxymethylcytosine (5hmC) is required for the tumorigenicity of glioblastoma cells. Fur
Externí odkaz:
https://doaj.org/article/6e167373836c4249903547f389fae70e
Autor:
Mayuko Yoda, Daniel Cifuentes, Natsuko Izumi, Yuriko Sakaguchi, Tsutomu Suzuki, Antonio J. Giraldez, Yukihide Tomari
Publikováno v:
Cell Reports, Vol 5, Iss 3, Pp 715-726 (2013)
MicroRNAs (miRNAs) are typically generated as ∼22-nucleotide double-stranded RNAs via the processing of precursor hairpins by the ribonuclease III enzyme Dicer, after which they are loaded into Argonaute (Ago) proteins to form an RNA-induced silenc
Externí odkaz:
https://doaj.org/article/3f51940f08d748979a1ab79a90f829a9
Publikováno v:
Nucleic Acids Research. 50:4713-4731
Contact-dependent growth inhibition is a mechanism of interbacterial competition mediated by delivery of the C-terminal toxin domain of CdiA protein (CdiA–CT) into neighboring bacteria. The CdiA–CT of enterohemorrhagic Escherichia coli EC869 (Cdi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0253c51c8542bec5b9de32e64869147
https://doi.org/10.1093/nar/gkac228
https://doi.org/10.1093/nar/gkac228
Autor:
Takayuki Ohira, Keiichi Minowa, Kei Sugiyama, Seisuke Yamashita, Yuriko Sakaguchi, Kenjyo Miyauchi, Ryo Noguchi, Akira Kaneko, Izumi Orita, Toshiaki Fukui, Kozo Tomita, Tsutomu Suzuki
Publikováno v:
Nature. 605:372-379
Post-transcriptional modifications have critical roles in tRNA stability and function1–4. In thermophiles, tRNAs are heavily modified to maintain their thermal stability under extreme growth temperatures5,6. Here we identified 2′-phosphouridine (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbab70fc2a603a50f3107a05c8749675
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100875903
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100875903
Autor:
Ryoya Nakagawa, Hisato Hirano, Satoshi N. Omura, Suchita Nety, Soumya Kannan, Han Altae-Tran, Xiao Yao, Yuriko Sakaguchi, Takayuki Ohira, Wen Y. Wu, Hiroshi Nakayama, Yutaro Shuto, Tatsuki Tanaka, Fumiya K. Sano, Tsukasa Kusakizako, Yoshiaki Kise, Yuzuru Itoh, Naoshi Dohmae, John van der Oost, Tsutomu Suzuki, Feng Zhang, Osamu Nureki
Publikováno v:
Nature 616 (2023) 7956
Nature, 616(7956), 390-397
Nature, 616(7956), 390-397
The class 2 type V CRISPR effector Cas12 is thought to have evolved from the IS200/IS605 superfamily of transposon-associated TnpB proteins1. Recent studies have identified TnpB proteins as miniature RNA-guided DNA endonucleases2,3. TnpB associates w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3678c60506fb09e5ce6035ba20014725
https://research.wur.nl/en/publications/cryo-em-structure-of-the-transposon-associated-tnpb-enzyme
https://research.wur.nl/en/publications/cryo-em-structure-of-the-transposon-associated-tnpb-enzyme
