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Simple prerequisite of presequence for mitochondrial protein import in the unicellular red alga Cyanidioschyzon merolae.
Hirata, Riko; Mogi, Yuko; Takahashi, Kohei; Nozaki, Hisayoshi; Higashiyama, Tetsuya; Yoshida, Yamato.
Afiliação
  • Hirata R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
  • Mogi Y; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
  • Takahashi K; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
  • Nozaki H; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
  • Higashiyama T; Biodiversity Division, National Institute for Environmental Studies, Ibaraki 305-8506, Japan.
  • Yoshida Y; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan.
J Cell Sci ; 137(14)2024 07 15.
Article em En | MEDLINE | ID: mdl-38940185
ABSTRACT
Mitochondrial biogenesis relies on hundreds of proteins that are derived from genes encoded in the nucleus. According to the characteristic properties of N-terminal targeting peptides (TPs) and multi-step authentication by the protein translocase called the TOM complex, nascent polypeptides satisfying the requirements are imported into mitochondria. However, it is unknown whether eukaryotic cells with a single mitochondrion per cell have a similar complexity of presequence requirements for mitochondrial protein import compared to other eukaryotes with multiple mitochondria. Based on putative mitochondrial TP sequences in the unicellular red alga Cyanidioschyzon merolae, we designed synthetic TPs and showed that functional TPs must have at least one basic residue and a specific amino acid composition, although their physicochemical properties are not strictly determined. Combined with the simple composition of the TOM complex in C. merolae, our results suggest that a regional positive charge in TPs is verified solely by TOM22 for mitochondrial protein import in C. merolae. The simple authentication mechanism indicates that the monomitochondrial C. merolae does not need to increase the cryptographic complexity of the lock-and-key mechanism for mitochondrial protein import.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transporte Proteico / Proteínas Mitocondriais / Rodófitas / Mitocôndrias Idioma: En Revista: J Cell Sci Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Transporte Proteico / Proteínas Mitocondriais / Rodófitas / Mitocôndrias Idioma: En Revista: J Cell Sci Ano de publicação: 2024 Tipo de documento: Article