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Journal of Bacteriology, September 2004, p. 6311-6315, Vol. 186, No. 18
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.18.6311-6315.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Claire Punginelli,¹ Bérengère Ize,^1,2 Nicola R. Stanley,^1,2, Valley Stewart,³ Gary Sawers,¹ Ben C. Berks,⁴ and Tracy Palmer^1,2*

Department of Molecular Microbiology, John Innes Centre,¹ School of Biological Sciences, University of East Anglia, Norwich,² Department of Biochemistry, University of Oxford, Oxford, United Kingdom,⁴ Section of Microbiology, University of California, Davis, California³

Received 14 May 2004/ Accepted 14 June 2004

Formate dehydrogenase N (FDH-N) of Escherichia coli is a membrane-bound enzyme comprising FdnG, FdnH, and FdnI subunits organized in an (ß)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.

Present address: Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, CA 90095-1489.

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