Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB

Toyoyuki Ose, Nicolas Soler, Linda Rasubala, Kimiko Kuroki, Daisuke Kohda, Dominique Fourmy, Satoko Yoshizawa, Katsumi Maenaka

    Research output: Contribution to journalArticle

    14 Citations (Scopus)

    Abstract

    Selenocysteine (Sec) is the "21st" amino acid and is genetically encoded by an unusual incorporation system. The stop codon UGA becomes a Sec codon when the selenocysteine insertion sequence (SECIS) exists downstream of UGA. Sec incorporation requires a specific elongation factor, SelB, which recognizes tRNASec via use of an EF-Tu-like domain and the SECIS mRNA hairpin via use of a C-terminal domain (SelB-C). SelB functions in multiple translational steps: binding to SECIS mRNA and tRNASec, delivery of tRNASec onto an A site, GTP hydrolysis, and release from tRNA and mRNA. However, this dynamic mechanism remains to be revealed. Here, we report a large domain rearrangement in the structure of SelB-C complexed with RNA. Surprisingly, the interdomain region forms new interactions with the phosphate backbone of a neighboring RNA, distinct from SECIS RNA binding. This SelB-RNA interaction is sequence independent, possibly reflecting SelB-tRNA/-rRNA recognitions. Based on these data, the dynamic SelB-ribosome-mRNA-tRNA interactions will be discussed.

    Original languageEnglish
    Pages (from-to)577-586
    Number of pages10
    JournalStructure
    Volume15
    Issue number5
    DOIs
    Publication statusPublished - May 16 2007

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    Selenocysteine
    Peptide Elongation Factors
    RNA
    Insertional Mutagenesis
    Transfer RNA
    Messenger RNA
    Peptide Elongation Factor Tu
    Terminator Codon
    Guanosine Triphosphate
    Ribosomes
    Codon
    Hydrolysis
    Phosphates
    Amino Acids

    All Science Journal Classification (ASJC) codes

    • Structural Biology
    • Molecular Biology

    Cite this

    Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB. / Ose, Toyoyuki; Soler, Nicolas; Rasubala, Linda; Kuroki, Kimiko; Kohda, Daisuke; Fourmy, Dominique; Yoshizawa, Satoko; Maenaka, Katsumi.

    In: Structure, Vol. 15, No. 5, 16.05.2007, p. 577-586.

    Research output: Contribution to journalArticle

    Ose, Toyoyuki ; Soler, Nicolas ; Rasubala, Linda ; Kuroki, Kimiko ; Kohda, Daisuke ; Fourmy, Dominique ; Yoshizawa, Satoko ; Maenaka, Katsumi. / Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB. In: Structure. 2007 ; Vol. 15, No. 5. pp. 577-586.
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