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

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

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Original languageEnglish
Pages6311-6315
Number of pages5
JournalJournal of Bacteriology
Journal publication date2004
Journal number18
Volume186
DOIs
StatePublished

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.

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