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

    18 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 Dive into the research topics of 'mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N'. Together they form a unique fingerprint.

  • Cite this