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mRNA Secondary Structure Modulates Translation of Tat-Dependent Formate Dehydrogenase N

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Punginelli, Claire | Ize, Bérengère | Stanley, Nicola | Stewart, Valley | Sawers, Gary | Berks, Ben | Palmer, Tracy

Edité par CCSD ; American Society for Microbiology -

International audience. ABSTRACT Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (αβγ) 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 (R 5 ) 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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