Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Nobukazu, Nameki"'
Autor:
Mayu Mikami, Hidehiko Shimizu, Norika Iwama, Mihono Yajima, Kanako Kuwasako, Yoshitoshi Ogura, Hyouta Himeno, Daisuke Kurita, Nobukazu Nameki
Publikováno v:
npj Antimicrobials and Resistance, Vol 2, Iss 1, Pp 1-14 (2024)
Abstract Escherichia coli possesses three stalled-ribosome rescue factors, tmRNA·SmpB (primary factor), ArfA (alternative factor to tmRNA·SmpB), and ArfB. Here, we examined the susceptibility of rescue factor-deficient strains from E. coli SE15 to
Externí odkaz:
https://doaj.org/article/5e5134b9f38049c79bcdcb91cb1bbde7
Autor:
Soichiro Hoshino, Ryohei Kanemura, Daisuke Kurita, Yukihiro Soutome, Hyouta Himeno, Masak Takaine, Masakatsu Watanabe, Nobukazu Nameki
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
Hoshino et al. show that PTH3, the S. cerevisiae homolog of C12orf65, is required for the translation of mitochondrial genes in the presence of antibiotics. This study suggests that PTH3 rescues the ribosomes stalled by antibiotics, playing a role in
Externí odkaz:
https://doaj.org/article/00aad6f4ead54b9485ea6826cd9557f7
Autor:
Nobukazu Nameki, Shin-ichi Terawaki, Masayuki Takizawa, Madoka Kitamura, Yutaka Muto, Kanako Kuwasako
Publikováno v:
The Journal of Biochemistry.
The pre-spliceosomal complex involves interactions between U1 and U2 snRNPs, where a ubiquitin-like domain (ULD) of SF3A1, a component of U2 snRNP, binds to the stem-loop 4 (SL4; the UUCG tetraloop) of U1 snRNA in U1 snRNP. Here, we reported the 1.80
Autor:
Kanako Kuwasako, Sakura Suzuki, Nobukazu Nameki, Masayuki Takizawa, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Satoru Watanabe, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Yutaka Muto
Publikováno v:
Biomolecular NMR Assignments. 16:297-303
Autor:
Nobukazu Nameki, Masayuki Takizawa, Takayuki Suzuki, Shoko Tani, Naohiro Kobayashi, Taiichi Sakamoto, Yutaka Muto, Kanako Kuwasako
Publikováno v:
Protein Science. 31
Autor:
Nobukazu, Nameki, Masayuki, Takizawa, Takayuki, Suzuki, Shoko, Tani, Naohiro, Kobayashi, Taiichi, Sakamoto, Yutaka, Muto, Kanako, Kuwasako
Publikováno v:
Protein science : a publication of the Protein Society. 31(10)
SURP domains are exclusively found in splicing-related proteins in all eukaryotes. SF3A1, a component of the U2 snRNP, has two tandem SURP domains, SURP1, and SURP2. SURP2 is permanently associated with a specific short region of SF3A3 within the SF3
Autor:
Daisuke Kurita, Soichiro Hoshino, Nobukazu Nameki, Yukihiro Soutome, Ryohei Kanemura, Masakatsu Watanabe, Hyouta Himeno, Masak Takaine
Publikováno v:
Communications Biology
Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
Mitochondrial translation appears to involve two stalled-ribosome rescue factors (srRFs). One srRF is an ICT1 protein from humans that rescues a “non-stop” type of mitochondrial ribosomes (mitoribosomes) stalled on mRNA lacking a stop codon, whil
Autor:
Masakiyo Sakaguchi, Megumi Akiyama, Chinatsu Saito, Tsukasa Maeda, Aoi Morimoto, Yusuke Inoue, Mana Kannari, Tsuyoshi Matsuta, Shota Sasaki, Frank J. Gonzalez, Takahiro Nakamura, Yuichi Tsuchida, Nobukazu Nameki
Publikováno v:
Journal of Biological Chemistry. 292:10574-10585
Hepatocyte nuclear factor 4α (HNF4α) controls the expression of liver-specific protein-coding genes. However, some microRNAs are also modulated by HNF4α, and it is not known whether they are direct targets of HNF4α and whether they influence hepa
Autor:
Seizo Takahashi, Makoto Inoue, Peter Güntert, Takaho Terada, Kanako Kuwasako, Takuhiro Ito, Kengo Tsuda, Nobukazu Nameki, Takanori Kigawa, Taiichi Sakamoto, Yutaka Muto, Naoya Tochio, Shigeyuki Yokoyama, Naohiro Kobayashi, Mikako Shirouzu, Kaori Wakamatsu, Mari Takahashi, Atsuko Sato
Publikováno v:
Protein Science. 26:280-291
The spliceosomal protein SF3b49, a component of the splicing factor 3b (SF3b) protein complex in the U2 small nuclear ribonucleoprotein, contains two RNA recognition motif (RRM) domains. In yeast, the first RRM domain (RRM1) of Hsh49 protein (yeast o
Autor:
Yuichiro Nomura, Akira Hirata, Takuya Kawamura, Tomoko Nagano, Nobukazu Nameki, Hiroyuki Hori, Takashi Yokogawa, Satoshi Ohno
Publikováno v:
Nucleic Acids Research
Archaeosine (G(+)), which is found only at position 15 in many archaeal tRNA, is formed by two steps, the replacement of the guanine base with preQ0 by archaeosine tRNA-guanine transglycosylase (ArcTGT) and the subsequent modification of preQ0 to G(+