mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. / Punginelli, Claire; Ize, Bérengère; Stanley, Nicola R.; Stewart, Valley; Sawers, Gary; Berks, Ben C.; Palmer, Tracy.
In: Journal of Bacteriology, Vol. 186, No. 18, 2004, p. 6311-6315.Research output: Contribution to journal › Article
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TY - JOUR
T1 - mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N
A1 - Punginelli,Claire
A1 - Ize,Bérengère
A1 - Stanley,Nicola R.
A1 - Stewart,Valley
A1 - Sawers,Gary
A1 - Berks,Ben C.
A1 - Palmer,Tracy
AU - Punginelli,Claire
AU - Ize,Bérengère
AU - Stanley,Nicola R.
AU - Stewart,Valley
AU - Sawers,Gary
AU - Berks,Ben C.
AU - Palmer,Tracy
PY - 2004
Y1 - 2004
N2 - 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.
AB - 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.
U2 - 10.1128/JB.186.18.6311-6315.2004
DO - 10.1128/JB.186.18.6311-6315.2004
M1 - Article
JO - Journal of Bacteriology
JF - Journal of Bacteriology
SN - 0021-9193
IS - 18
VL - 186
SP - 6311
EP - 6315
ER -