mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

Claire Punginelli, Bérengère Ize, Nicola R. Stanley, Valley Stewart, Gary Sawers, Ben C. Berks, Tracy Palmer

    Research output: Contribution to journalArticle

    15 Citations (Scopus)

    Abstract

    Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.
    Original languageEnglish
    Pages (from-to)6311-6315
    Number of pages5
    JournalJournal of Bacteriology
    Volume186
    Issue number18
    DOIs
    Publication statusPublished - 2004

    Fingerprint

    Formate Dehydrogenases
    Protein Sorting Signals
    Arginine
    Messenger RNA
    Membranes
    Computational Biology
    Codon
    Proteins
    Escherichia coli
    Amino Acids
    Enzymes

    Cite this

    Punginelli, Claire ; Ize, Bérengère ; Stanley, Nicola R. ; Stewart, Valley ; Sawers, Gary ; Berks, Ben C. ; Palmer, Tracy. / mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. In: Journal of Bacteriology. 2004 ; Vol. 186, No. 18. pp. 6311-6315.
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    abstract = "Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.",
    author = "Claire Punginelli and B{\'e}reng{\`e}re Ize and Stanley, {Nicola R.} and Valley Stewart and Gary Sawers and Berks, {Ben C.} and Tracy Palmer",
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    mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. / Punginelli, Claire; Ize, Bérengère; Stanley, Nicola R.; Stewart, Valley; Sawers, Gary; Berks, Ben C.; Palmer, Tracy.

    In: Journal of Bacteriology, Vol. 186, No. 18, 2004, p. 6311-6315.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N

    AU - Punginelli, Claire

    AU - Ize, Bérengère

    AU - Stanley, Nicola R.

    AU - Stewart, Valley

    AU - Sawers, Gary

    AU - Berks, Ben C.

    AU - Palmer, Tracy

    PY - 2004

    Y1 - 2004

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    AB - Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (alphabetagamma)3 configuration. The FdnG subunit carries a Tat-dependent signal peptide, which localizes the protein complex to the periplasmic side of the membrane. We noted that substitution of the first arginine (R5) in the twin arginine signal sequence of FdnG for a variety of other amino acids resulted in a dramatic (up to 60-fold) increase in the levels of protein synthesized. Bioinformatic analysis suggested that the mRNA specifying the first 17 codons of fdnG forms a stable stem-loop structure. A detailed mutational analysis has demonstrated the importance of this mRNA stem-loop in modulating FDH-N translation.

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    DO - 10.1128/JB.186.18.6311-6315.2004

    M3 - Article

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    JO - Journal of Bacteriology

    JF - Journal of Bacteriology

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