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

Content Provider	PubMed Central
Author	Claire, Punginelli Ize, Bérengère Stanley, Nicola R. Stewart, Valley Sawers, Gary Berks, Ben C. Palmer, Tracy
Copyright Year	2004
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 (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.
Related Links	http://dx.doi.org/10.1128/jb.186.18.6311-6315.2004
Ending Page	6315
Page Count	5
Starting Page	6311
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	18
Volume Number	186
Language	English
Publisher	American Society for Microbiology
Publisher Date	2004-09-15
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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