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

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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 journalArticle

Harvard

Punginelli, C, Ize, B, Stanley, NR, Stewart, V, Sawers, G, Berks, BC & Palmer, T 2004, 'mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N' Journal of Bacteriology, vol 186, no. 18, pp. 6311-6315.

APA

Punginelli, C., Ize, B., Stanley, N. R., Stewart, V., Sawers, G., Berks, B. C., & Palmer, T. (2004). mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. Journal of Bacteriology, 186(18), 6311-6315doi: 10.1128/JB.186.18.6311-6315.2004

Vancouver

Punginelli C, Ize B, Stanley NR, Stewart V, Sawers G, Berks BC et al. mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N. Journal of Bacteriology. 2004;186(18):6311-6315.

Author

Punginelli, Claire; Ize, Bérengère; Stanley, Nicola R.; Stewart, Valley; Sawers, Gary; Berks, Ben C.; Palmer, Tracy / mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N.

In: Journal of Bacteriology, Vol. 186, No. 18, 2004, p. 6311-6315.

Research output: Contribution to journalArticle

Bibtex - Download

@article{fdb08f84edb547ac9bcbe3ccd49b1fee,
title = "mRNA secondary structure modulates translation of Tat-dependent formate dehydrogenase N",
author = "Claire Punginelli and Bérengère Ize and Stanley, {Nicola R.} and Valley Stewart and Gary Sawers and Berks, {Ben C.} and Tracy Palmer",
year = "2004",
volume = "186",
number = "18",
pages = "6311--6315",
journal = "Journal of Bacteriology",
issn = "0021-9193",

}

RIS (suitable for import to EndNote) - Download

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 -

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