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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 publication

DOI

10.1128/JB.186.18.6311-6315.2004

Type

Journal article

Journal

J Bacteriol

Publication Date

09/2004

Volume

186

Pages

6311 - 6315

Keywords

Artificial Gene Fusion, Base Sequence, DNA Mutational Analysis, Escherichia coli, Escherichia coli Proteins, Formate Dehydrogenases, Genes, Reporter, Molecular Sequence Data, Nucleic Acid Conformation, Periplasmic Proteins, Protein Biosynthesis, RNA, Bacterial, RNA, Messenger, beta-Galactosidase