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Mechanistic dissection of premature translation termination induced by acidic residues-enriched nascent peptide.
Chadani, Yuhei; Kanamori, Takashi; Niwa, Tatsuya; Ichihara, Kazuya; Nakayama, Keiichi I; Matsumoto, Akinobu; Taguchi, Hideki.
Afiliação
  • Chadani Y; Faculty of Environmental, Life, Natural Science and Technology, Okayama University, Okayama 700-8530, Japan. Electronic address: ychadani@okayama-u.ac.jp.
  • Kanamori T; GeneFrontier Corporation, Kashiwa-shi, Chiba 277-0005, Japan.
  • Niwa T; Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
  • Ichihara K; Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
  • Nakayama KI; Anticancer Strategies Laboratory, TMDU Advanced Research Institute, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo 113-8510, Japan; Division of Cell Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
  • Matsumoto A; Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
  • Taguchi H; Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8503, Japan. Electronic address: taguchi@bio.titech.ac.jp.
Cell Rep ; 42(12): 113569, 2023 12 26.
Article em En | MEDLINE | ID: mdl-38071619
ABSTRACT
Ribosomes polymerize nascent peptides through repeated inter-subunit rearrangements between the classic and hybrid states. The peptidyl-tRNA, the intermediate species during translation elongation, stabilizes the translating ribosome to ensure robust continuity of elongation. However, the translation of acidic residue-rich sequences destabilizes the ribosome, leading to a stochastic premature translation cessation termed intrinsic ribosome destabilization (IRD), which is still ill-defined. Here, we dissect the molecular mechanisms underlying IRD in Escherichia coli. Reconstitution of the IRD event reveals that (1) the prolonged ribosome stalling enhances IRD-mediated translation discontinuation, (2) IRD depends on temperature, (3) the destabilized 70S ribosome complex is not necessarily split, and (4) the destabilized ribosome is subjected to peptidyl-tRNA hydrolase-mediated hydrolysis of the peptidyl-tRNA without subunit splitting or recycling factors-mediated subunit splitting. Collectively, our data indicate that the translation of acidic-rich sequences alters the conformation of the 70S ribosome to an aberrant state that allows the noncanonical premature termination.
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Texto completo: 1 Coleções: 01-internacional Contexto em Saúde: 3_ND Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Proteínas de Escherichia coli Idioma: En Revista: Cell Rep Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Contexto em Saúde: 3_ND Base de dados: MEDLINE Assunto principal: Biossíntese de Proteínas / Proteínas de Escherichia coli Idioma: En Revista: Cell Rep Ano de publicação: 2023 Tipo de documento: Article